Lewis E. Kay - Publications

Affiliations: 
Biochemistry University of Toronto, Toronto, ON, Canada 
Area:
Development and Application of NMR Methods for The Study of Protein Structure and Dynamics
Website:
http://biochemistry.utoronto.ca/person/lewis-e-kay/

263 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2019 Kim TH, Tsang B, Vernon RM, Sonenberg N, Kay LE, Forman-Kay JD. Phospho-dependent phase separation of FMRP and CAPRIN1 recapitulates regulation of translation and deadenylation. Science (New York, N.Y.). 365: 825-829. PMID 31439799 DOI: 10.1126/science.aax4240  0.32
2019 Rennella E, Morgan GJ, Yan N, Kelly JW, Kay LE. The role of protein thermodynamics and primary structure in fibrillogenesis of variable domains from immunoglobulin light-chains. Journal of the American Chemical Society. PMID 31364359 DOI: 10.1021/jacs.9b05499  0.4
2019 Morgan GJ, Yan NL, Mortenson DE, Rennella E, Blundon JM, Gwin RM, Lin CY, Stanfield RL, Brown SJ, Rosen H, Spicer TP, Fernandez-Vega V, Merlini G, Kay LE, Wilson IA, et al. Stabilization of amyloidogenic immunoglobulin light chains by small molecules. Proceedings of the National Academy of Sciences of the United States of America. PMID 30971495 DOI: 10.1073/pnas.1817567116  0.4
2019 Sekhar A, Kay LE. An NMR View of Protein Dynamics in Health and Disease. Annual Review of Biophysics. PMID 30901260 DOI: 10.1146/annurev-biophys-052118-115647  0.6
2019 Yuwen T, Huang R, Vallurupalli P, Kay LE. A Methyl-TROSY Based ¹H Relaxation Dispersion Experiment for Studies of Conformational Exchange in High Molecular Weight Proteins. Angewandte Chemie (International Ed. in English). PMID 30847985 DOI: 10.1002/anie.201900241  0.64
2018 Rennella E, Morgan GJ, Kelly JW, Kay LE. Role of domain interactions in the aggregation of full-length immunoglobulin light chains. Proceedings of the National Academy of Sciences of the United States of America. PMID 30598439 DOI: 10.1073/pnas.1817538116  0.4
2018 Huang R, Ripstein ZA, Rubinstein JL, Kay LE. Cooperative subunit dynamics modulate p97 function. Proceedings of the National Academy of Sciences of the United States of America. PMID 30584095 DOI: 10.1073/pnas.1815495116  0.64
2018 Yuwen T, Sekhar A, Baldwin AJ, Vallurupalli P, Kay LE. Measuring Diffusion Constants of Invisible Protein Conformers by Triple-Quantum ¹H CPMG Relaxation Dispersion. Angewandte Chemie (International Ed. in English). PMID 30370966 DOI: 10.1002/anie.201810868  0.64
2018 Gopalan AB, Yuwen T, Kay LE, Vallurupalli P. A methyl H double quantum CPMG experiment to study protein conformational exchange. Journal of Biomolecular Nmr. PMID 30276607 DOI: 10.1007/s10858-018-0208-z  0.64
2018 Yuwen T, Bah A, Brady JP, Ferrage F, Bouvignies G, Kay LE. Measuring Solvent Hydrogen Exchange Rates by Multi-Frequency Excitation N CEST. The Journal of Physical Chemistry. B. PMID 30179470 DOI: 10.1021/acs.jpcb.8b06820  0.64
2018 Boisbouvier J, Kay LE. Advanced isotopic labeling for the NMR investigation of challenging proteins and nucleic acids. Journal of Biomolecular Nmr. PMID 30043256 DOI: 10.1007/s10858-018-0199-9  0.36
2018 Vahidi S, Ripstein ZA, Bonomi M, Yuwen T, Mabanglo MF, Juravsky JB, Rizzolo K, Velyvis A, Houry WA, Vendruscolo M, Rubinstein JL, Kay LE. Reversible inhibition of the ClpP protease via an N-terminal conformational switch. Proceedings of the National Academy of Sciences of the United States of America. PMID 29941580 DOI: 10.1073/pnas.1805125115  0.64
2018 Mondal J, Ahalawat N, Pandit S, Kay LE, Vallurupalli P. Atomic resolution mechanism of ligand binding to a solvent inaccessible cavity in T4 lysozyme. Plos Computational Biology. 14: e1006180. PMID 29775455 DOI: 10.1371/journal.pcbi.1006180  0.48
2018 Yuwen T, Bouvignies G, Kay LE. Exploring methods to expedite the recording of CEST datasets using selective pulse excitation. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 292: 1-7. PMID 29753980 DOI: 10.1016/j.jmr.2018.04.013  0.64
2018 Augustyniak R, Kay LE. Cotranslocational processing of the protein substrate calmodulin by an AAA+ unfoldase occurs via unfolding and refolding intermediates. Proceedings of the National Academy of Sciences of the United States of America. PMID 29735657 DOI: 10.1073/pnas.1721811115  0.4
2018 Yuwen T, Kay LE, Bouvignies G. Dramatic Decrease in CEST Measurement Times Using Multi-site Excitation. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 29663694 DOI: 10.1002/cphc.201800249  0.64
2018 Kitevski-LeBlanc JL, Yuwen T, Dyer PN, Rudolph J, Luger K, Kay LE. Investigating the Dynamics of Destabilized Nucleosomes Using Methyl-TROSY NMR. Journal of the American Chemical Society. PMID 29589929 DOI: 10.1021/jacs.8b00931  0.64
2018 Culik RM, Sekhar A, Nagesh J, Deol H, Rumfeldt JAO, Meiering EM, Kay LE. Effects of maturation on the conformational free-energy landscape of SOD1. Proceedings of the National Academy of Sciences of the United States of America. PMID 29483249 DOI: 10.1073/pnas.1721022115  0.6
2018 Sekhar A, Velyvis A, Zoltsman G, Rosenzweig R, Bouvignies G, Kay LE. Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions. Elife. 7. PMID 29460778 DOI: 10.7554/eLife.32764  0.6
2018 Yuwen T, Kay LE. A new class of CEST experiment based on selecting different magnetization components at the start and end of the CEST relaxation element: an application to 1H CEST. Journal of Biomolecular Nmr. PMID 29352366 DOI: 10.1007/s10858-017-0161-2  0.64
2018 Yuwen T, Brady JP, Kay LE. Probing conformational exchange in weakly interacting, slowly exchanging protein systems via off-resonance R1ρ experiments: Application to studies of protein phase separation. Journal of the American Chemical Society. PMID 29303268 DOI: 10.1021/jacs.7b09576  0.64
2017 Huang R, Pérez F, Kay LE. Probing the cooperativity of Thermoplasma acidophilum proteasome core particle gating by NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. PMID 29087330 DOI: 10.1073/pnas.1712297114  0.64
2017 Brady JP, Farber PJ, Sekhar A, Lin YH, Huang R, Bah A, Nott TJ, Chan HS, Baldwin AJ, Forman-Kay JD, Kay LE. Structural and hydrodynamic properties of an intrinsically disordered region of a germ cell-specific protein on phase separation. Proceedings of the National Academy of Sciences of the United States of America. PMID 28894006 DOI: 10.1073/pnas.1706197114  0.64
2017 Sekhar A, Nagesh J, Rosenzweig R, Kay LE. Conformational heterogeneity in the Hsp70 chaperone-substrate ensemble: identified from analysis of NMR-detected titration data. Protein Science : a Publication of the Protein Society. PMID 28833766 DOI: 10.1002/pro.3276  0.6
2017 Schütz AK, Rennella E, Kay LE. Exploiting conformational plasticity in the AAA+ protein VCP/p97 to modify function. Proceedings of the National Academy of Sciences of the United States of America. PMID 28760999 DOI: 10.1073/pnas.1707974114  0.4
2017 Huang R, Brady JP, Sekhar A, Yuwen T, Kay LE. An enhanced sensitivity methyl (1)H triple-quantum pulse scheme for measuring diffusion constants of macromolecules. Journal of Biomolecular Nmr. PMID 28717997 DOI: 10.1007/s10858-017-0122-9  0.64
2017 Rosenzweig R, Sekhar A, Nagesh J, Kay LE. Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles. Elife. 6. PMID 28708484 DOI: 10.7554/eLife.28030  0.6
2017 Yuwen T, Huang R, Kay LE. Probing slow timescale dynamics in proteins using methyl (1)H CEST. Journal of Biomolecular Nmr. PMID 28647789 DOI: 10.1007/s10858-017-0121-x  0.64
2017 Malevanets A, Chong PA, Hansen DF, Rizk P, Sun Y, Lin H, Muhandiram R, Chakrabartty A, Kay LE, Forman-Kay JD, Wodak SJ. Interplay of buried histidine protonation and protein stability in prion misfolding. Scientific Reports. 7: 882. PMID 28408762 DOI: 10.1038/s41598-017-00954-7  0.44
2017 Kitevski-LeBlanc J, Fradet-Turcotte A, Kukic P, Wilson MD, Portella G, Yuwen T, Panier S, Duan S, Canny MD, van Ingen H, Arrowsmith CH, Rubinstein JL, Vendruscolo M, Durocher D, Kay LE. The RNF168 paralog RNF169 defines a new class of ubiquitylated-histone reader involved in the response to DNA damage. Elife. 6. PMID 28406400 DOI: 10.7554/eLife.23872  0.64
2017 Ripstein ZA, Huang R, Augustyniak R, Kay LE, Rubinstein JL. Structure of a AAA+ unfoldase in the process of unfolding substrate. Elife. 6. PMID 28390173 DOI: 10.7554/eLife.25754  0.64
2017 Yuwen T, Kay LE. Longitudinal relaxation optimized amide (1)H-CEST experiments for studying slow chemical exchange processes in fully protonated proteins. Journal of Biomolecular Nmr. PMID 28357518 DOI: 10.1007/s10858-017-0104-y  0.64
2017 Valluruapalli P, Sekhar A, Yuwen T, Kay LE. Probing conformational dynamics in biomolecules via chemical exchange saturation transfer: a primer. Journal of Biomolecular Nmr. PMID 28317074 DOI: 10.1007/s10858-017-0099-4  0.64
2017 Borkar AN, Vallurupalli P, Camilloni C, Kay LE, Vendruscolo M. Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop. Physical Chemistry Chemical Physics : Pccp. PMID 28067358 DOI: 10.1039/c6cp08313g  0.48
2017 Rennella E, Sekhar A, Kay LE. Self-Assembly of Human Profilin-1 Detected by CPMG NMR Spectroscopy. Biochemistry. PMID 28052669 DOI: 10.1021/acs.biochem.6b01263  0.6
2016 Vallurupalli P, Chakrabarti N, Pomès R, Kay LE. Atomistic picture of conformational exchange in a T4 lysozyme cavity mutant: an experiment-guided molecular dynamics study. Chemical Science. 7: 3602-3613. PMID 30008994 DOI: 10.1039/c5sc03886c  0.48
2016 Yuwen T, Sekhar A, Kay LE. Separating Dipolar and Chemical Exchange Magnetization Transfer Processes in (1) H-CEST. Angewandte Chemie (International Ed. in English). PMID 28035783 DOI: 10.1002/anie.201610759  0.64
2016 Sekhar A, Rumfeldt JA, Broom HR, Doyle CM, Sobering RE, Meiering EM, Kay LE. Probing the free energy landscapes of ALS disease mutants of SOD1 by NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. PMID 27791136 DOI: 10.1073/pnas.1611418113  0.6
2016 Yuwen T, Vallurupalli P, Kay LE. Enhancing the Sensitivity of CPMG Relaxation Dispersion to Conformational Exchange Processes by Multiple-Quantum Spectroscopy. Angewandte Chemie (International Ed. in English). PMID 27527986 DOI: 10.1002/anie.201605843  0.64
2016 Yuwen T, Sekhar A, Kay LE. Evaluating the influence of initial magnetization conditions on extracted exchange parameters in NMR relaxation experiments: applications to CPMG and CEST. Journal of Biomolecular Nmr. PMID 27473413 DOI: 10.1007/s10858-016-0045-x  0.64
2016 Huang R, Ripstein ZA, Augustyniak R, Lazniewski M, Ginalski K, Kay LE, Rubinstein JL. Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study. Proceedings of the National Academy of Sciences of the United States of America. PMID 27402735 DOI: 10.1073/pnas.1603980113  1
2016 Rennella E, Schuetz AK, Kay LE. Quantitative measurement of exchange dynamics in proteins via (13)C relaxation dispersion of (13)CHD2-labeled samples. Journal of Biomolecular Nmr. PMID 27251650 DOI: 10.1007/s10858-016-0038-9  0.4
2016 Sekhar A, Rosenzweig R, Bouvignies G, Kay LE. Hsp70 biases the folding pathways of client proteins. Proceedings of the National Academy of Sciences of the United States of America. PMID 27140645 DOI: 10.1073/pnas.1601846113  0.6
2016 Doyle CM, Rumfeldt JA, Broom HR, Sekhar A, Kay LE, Meiering EM. Concurrent Increases and Decreases in Local Stability and Conformational Heterogeneity in Cu, Zn Superoxide Dismutase Variants Revealed by Temperature-Dependence of Amide Chemical Shifts. Biochemistry. PMID 26849066 DOI: 10.1021/acs.biochem.5b01133  0.6
2015 Rosenzweig R, Kay LE. Solution NMR Spectroscopy Provides an Avenue for the Study of Functionally Dynamic Molecular Machines: The Example of Protein Disaggregation. Journal of the American Chemical Society. PMID 26651836 DOI: 10.1021/jacs.5b11346  1
2015 Rosenzweig R, Farber P, Velyvis A, Rennella E, Latham MP, Kay LE. ClpB N-terminal domain plays a regulatory role in protein disaggregation. Proceedings of the National Academy of Sciences of the United States of America. PMID 26621746 DOI: 10.1073/pnas.1512783112  1
2015 Rennella E, Huang R, Velyvis A, Kay LE. (13)CHD2-CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins. Journal of Biomolecular Nmr. 63: 187-99. PMID 26271302 DOI: 10.1007/s10858-015-9974-z  1
2015 Sekhar A, Rosenzweig R, Bouvignies G, Kay LE. Mapping the conformation of a client protein through the Hsp70 functional cycle. Proceedings of the National Academy of Sciences of the United States of America. 112: 10395-400. PMID 26240333 DOI: 10.1073/pnas.1508504112  1
2015 Long D, Delaglio F, Sekhar A, Kay LE. Probing Invisible, Excited Protein States by Non-Uniformly Sampled Pseudo-4D CEST Spectroscopy. Angewandte Chemie (International Ed. in English). 54: 10507-11. PMID 26178142 DOI: 10.1002/anie.201504070  1
2015 Sekhar A, Bain AD, Rumfeldt JA, Meiering EM, Kay LE. Evolution of magnetization due to asymmetric dimerization: theoretical considerations and application to aberrant oligomers formed by apoSOD1(2SH). Physical Chemistry Chemical Physics : Pccp. PMID 26156673 DOI: 10.1039/c5cp03044g  1
2015 Borkar AN, Vallurupalli P, Camilloni C, Kay LE, Vendruscolo M. 89 Constructing free energy landscapes of RNAs at atomic resolution and characterisation of their excited states. Journal of Biomolecular Structure & Dynamics. 33: 58. PMID 26103301 DOI: 10.1080/07391102.2015.1032706  0.48
2015 Sekhar A, Rumfeldt JA, Broom HR, Doyle CM, Bouvignies G, Meiering EM, Kay LE. Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways. Elife. 4. PMID 26099300 DOI: 10.7554/eLife.07296  1
2015 Bah A, Vernon RM, Siddiqui Z, Krzeminski M, Muhandiram R, Zhao C, Sonenberg N, Kay LE, Forman-Kay JD. Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch. Nature. 519: 106-9. PMID 25533957 DOI: 10.1038/nature13999  0.44
2014 Long D, Sekhar A, Kay LE. Triple resonance-based ¹³C(α) and ¹³C(β) CEST experiments for studies of ms timescale dynamics in proteins. Journal of Biomolecular Nmr. 60: 203-8. PMID 25348177 DOI: 10.1007/s10858-014-9868-5  1
2014 Latham MP, Kay LE. A similar in vitro and in cell lysate folding intermediate for the FF domain. Journal of Molecular Biology. 426: 3214-20. PMID 25083919 DOI: 10.1016/j.jmb.2014.07.019  1
2014 Rosenzweig R, Kay LE. Bringing dynamic molecular machines into focus by methyl-TROSY NMR. Annual Review of Biochemistry. 83: 291-315. PMID 24905784 DOI: 10.1146/annurev-biochem-060713-035829  1
2014 Long D, Bouvignies G, Kay LE. Measuring hydrogen exchange rates in invisible protein excited states. Proceedings of the National Academy of Sciences of the United States of America. 111: 8820-5. PMID 24889628 DOI: 10.1073/pnas.1405011111  0.44
2014 Sanchez-Medina C, Sekhar A, Vallurupalli P, Cerminara M, Muñoz V, Kay LE. Probing the free energy landscape of the fast-folding gpW protein by relaxation dispersion NMR. Journal of the American Chemical Society. 136: 7444-51. PMID 24805164 DOI: 10.1021/ja502705y  1
2014 Hansen AL, Kay LE. Measurement of histidine pKa values and tautomer populations in invisible protein states. Proceedings of the National Academy of Sciences of the United States of America. 111: E1705-12. PMID 24733918 DOI: 10.1073/pnas.1400577111  1
2014 Sekhar A, Latham MP, Vallurupalli P, Kay LE. Viscosity-dependent kinetics of protein conformational exchange: microviscosity effects and the need for a small viscogen. The Journal of Physical Chemistry. B. 118: 4546-51. PMID 24707961 DOI: 10.1021/jp501583t  1
2014 Latham MP, Sekhar A, Kay LE. Understanding the mechanism of proteasome 20S core particle gating. Proceedings of the National Academy of Sciences of the United States of America. 111: 5532-7. PMID 24706783 DOI: 10.1073/pnas.1322079111  1
2014 Kay LE, Frydman L. A special "JMR Perspectives" issue: foresights in biomolecular solution-state NMR spectroscopy - from spin gymnastics to structure and dynamics. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 241: 1-2. PMID 24656075 DOI: 10.1016/j.jmr.2014.01.010  1
2014 Shi L, Kay LE. Tracing an allosteric pathway regulating the activity of the HslV protease. Proceedings of the National Academy of Sciences of the United States of America. 111: 2140-5. PMID 24469799 DOI: 10.1073/pnas.1318476111  1
2014 Wang X, Vallurupalli P, Vu A, Lee K, Sun S, Bai WJ, Wu C, Zhou H, Shea JE, Kay LE, Dahlquist FW. The linker between the dimerization and catalytic domains of the CheA histidine kinase propagates changes in structure and dynamics that are important for enzymatic activity. Biochemistry. 53: 855-61. PMID 24444349 DOI: 10.1021/bi4012379  0.76
2014 Bouvignies G, Vallurupalli P, Kay LE. Visualizing side chains of invisible protein conformers by solution NMR. Journal of Molecular Biology. 426: 763-74. PMID 24211467 DOI: 10.1016/j.jmb.2013.10.041  1
2013 Pocanschi CL, Ehsani S, Mehrabian M, Wille H, Reginold W, Trimble WS, Wang H, Yee A, Arrowsmith CH, Bozóky Z, Kay LE, Forman-Kay JD, Rini JM, Schmitt-Ulms G. The ZIP5 ectodomain co-localizes with PrP and may acquire a PrP-like fold that assembles into a dimer. Plos One. 8: e72446. PMID 24039764 DOI: 10.1371/journal.pone.0072446  1
2013 Long D, Marshall CB, Bouvignies G, Mazhab-Jafari MT, Smith MJ, Ikura M, Kay LE. A comparative CEST NMR study of slow conformational dynamics of small GTPases complexed with GTP and GTP analogues. Angewandte Chemie (International Ed. in English). 52: 10771-4. PMID 24039022 DOI: 10.1002/anie.201305434  1
2013 Mainz A, Religa TL, Sprangers R, Linser R, Kay LE, Reif B. NMR spectroscopy of soluble protein complexes at one mega-dalton and beyond. Angewandte Chemie (International Ed. in English). 52: 8746-51. PMID 23873792 DOI: 10.1002/anie.201301215  1
2013 Sekhar A, Kay LE. NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers. Proceedings of the National Academy of Sciences of the United States of America. 110: 12867-74. PMID 23868852 DOI: 10.1073/pnas.1305688110  1
2013 Sekhar A, Vallurupalli P, Kay LE. Defining a length scale for millisecond-timescale protein conformational exchange. Proceedings of the National Academy of Sciences of the United States of America. 110: 11391-6. PMID 23801755 DOI: 10.1073/pnas.1303273110  0.4
2013 Velyvis A, Kay LE. Measurement of active site ionization equilibria in the 670 kDa proteasome core particle using methyl-TROSY NMR. Journal of the American Chemical Society. 135: 9259-62. PMID 23800213 DOI: 10.1021/ja403091c  1
2013 Vallurupalli P, Bouvignies G, Kay LE. A computational study of the effects of (13) C-(13) C scalar couplings on (13) C CEST NMR spectra: towards studies on a uniformly (13) C-labeled protein. Chembiochem : a European Journal of Chemical Biology. 14: 1709-13. PMID 23784752 DOI: 10.1002/cbic.201300230  1
2013 Tugarinov V, Kay LE. Estimating side-chain order in [U-2H;13CH3]-labeled high molecular weight proteins from analysis of HMQC/HSQC spectra. The Journal of Physical Chemistry. B. 117: 3571-7. PMID 23458382 DOI: 10.1021/jp401088c  1
2013 Vallurupalli P, Kay LE. Probing slow chemical exchange at carbonyl sites in proteins by chemical exchange saturation transfer NMR spectroscopy. Angewandte Chemie (International Ed. in English). 52: 4156-9. PMID 23450751 DOI: 10.1002/anie.201209118  1
2013 Mazhab-Jafari MT, Marshall CB, Stathopulos PB, Kobashigawa Y, Stambolic V, Kay LE, Inagaki F, Ikura M. Membrane-dependent modulation of the mTOR activator Rheb: NMR observations of a GTPase tethered to a lipid-bilayer nanodisc. Journal of the American Chemical Society. 135: 3367-70. PMID 23409921 DOI: 10.1021/ja312508w  1
2013 Rosenzweig R, Moradi S, Zarrine-Afsar A, Glover JR, Kay LE. Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction. Science (New York, N.Y.). 339: 1080-3. PMID 23393091 DOI: 10.1126/science.1233066  1
2013 Hansen AL, Bouvignies G, Kay LE. Probing slowly exchanging protein systems via ¹³Cα-CEST: monitoring folding of the Im7 protein. Journal of Biomolecular Nmr. 55: 279-89. PMID 23386228 DOI: 10.1007/s10858-013-9711-4  1
2013 Baldwin AJ, Kay LE. An R(1ρ) expression for a spin in chemical exchange between two sites with unequal transverse relaxation rates. Journal of Biomolecular Nmr. 55: 211-8. PMID 23340732 DOI: 10.1007/s10858-012-9694-6  1
2013 Latham MP, Kay LE. Probing non-specific interactions of Ca²⁺-calmodulin in E. coli lysate. Journal of Biomolecular Nmr. 55: 239-47. PMID 23324860 DOI: 10.1007/s10858-013-9705-2  1
2012 Bouvignies G, Kay LE. Measurement of proton chemical shifts in invisible states of slowly exchanging protein systems by chemical exchange saturation transfer. The Journal of Physical Chemistry. B. 116: 14311-7. PMID 23194058 DOI: 10.1021/jp311109u  1
2012 Ruschak AM, Kay LE. Proteasome allostery as a population shift between interchanging conformers. Proceedings of the National Academy of Sciences of the United States of America. 109: E3454-62. PMID 23150576 DOI: 10.1073/pnas.1213640109  1
2012 Sekhar A, Vallurupalli P, Kay LE. Folding of the four-helix bundle FF domain from a compact on-pathway intermediate state is governed predominantly by water motion. Proceedings of the National Academy of Sciences of the United States of America. 109: 19268-73. PMID 23129654 DOI: 10.1073/pnas.1212036109  1
2012 Latham MP, Kay LE. Is buffer a good proxy for a crowded cell-like environment? A comparative NMR study of calmodulin side-chain dynamics in buffer and E. coli lysate. Plos One. 7: e48226. PMID 23118958 DOI: 10.1371/journal.pone.0048226  1
2012 Velyvis A, Ruschak AM, Kay LE. An economical method for production of (2)H, (13)CH3-threonine for solution NMR studies of large protein complexes: application to the 670 kDa proteasome. Plos One. 7: e43725. PMID 22984438 DOI: 10.1371/journal.pone.0043725  1
2012 Markley JL, Akutsu H, Asakura T, Baldus M, Boelens R, Bonvin A, Kaptein R, Bax A, Bezsonova I, Gryk MR, Hoch JC, Korzhnev DM, Maciejewski MW, Case D, Chazin WJ, ... ... Kay LE, et al. In support of the BMRB. Nature Structural & Molecular Biology. 19: 854-60. PMID 22955930 DOI: 10.1038/nsmb.2371  0.6
2012 Baldwin AJ, Walsh P, Hansen DF, Hilton GR, Benesch JL, Sharpe S, Kay LE. Probing dynamic conformations of the high-molecular-weight αB-crystallin heat shock protein ensemble by NMR spectroscopy. Journal of the American Chemical Society. 134: 15343-50. PMID 22916679 DOI: 10.1021/ja307874r  1
2012 Baldwin AJ, Kay LE. Structural biology: Dynamic binding. Nature. 488: 165-6. PMID 22874961 DOI: 10.1038/488165a  1
2012 Kupče E, Kay LE. Parallel acquisition of multi-dimensional spectra in protein NMR. Journal of Biomolecular Nmr. 54: 1-7. PMID 22802131 DOI: 10.1007/s10858-012-9646-1  1
2012 Bouvignies G, Kay LE. A 2D ¹³C-CEST experiment for studying slowly exchanging protein systems using methyl probes: an application to protein folding. Journal of Biomolecular Nmr. 53: 303-10. PMID 22689067 DOI: 10.1007/s10858-012-9640-7  1
2012 Korzhnev DM, Religa TL, Kay LE. Transiently populated intermediate functions as a branching point of the FF domain folding pathway. Proceedings of the National Academy of Sciences of the United States of America. 109: 17777-82. PMID 22647611 DOI: 10.1073/pnas.1201799109  1
2012 Vallurupalli P, Bouvignies G, Kay LE. Studying "invisible" excited protein states in slow exchange with a major state conformation. Journal of the American Chemical Society. 134: 8148-61. PMID 22554188 DOI: 10.1021/ja3001419  1
2012 Neudecker P, Robustelli P, Cavalli A, Walsh P, Lundström P, Zarrine-Afsar A, Sharpe S, Vendruscolo M, Kay LE. Structure of an intermediate state in protein folding and aggregation. Science (New York, N.Y.). 336: 362-6. PMID 22517863 DOI: 10.1126/science.1214203  1
2012 Baldwin AJ, Kay LE. Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R(1ρ): an application to αB-crystallin. Journal of Biomolecular Nmr. 53: 1-12. PMID 22476760 DOI: 10.1007/s10858-012-9617-6  1
2012 Hansen AL, Lundström P, Velyvis A, Kay LE. Quantifying millisecond exchange dynamics in proteins by CPMG relaxation dispersion NMR using side-chain 1H probes. Journal of the American Chemical Society. 134: 3178-89. PMID 22300166 DOI: 10.1021/ja210711v  1
2012 Barette J, Velyvis A, Religa TL, Korzhnev DM, Kay LE. Cross-validation of the structure of a transiently formed and low populated FF domain folding intermediate determined by relaxation dispersion NMR and CS-Rosetta. The Journal of Physical Chemistry. B. 116: 6637-44. PMID 22148426 DOI: 10.1021/jp209974f  1
2011 Baldwin AJ, Lioe H, Hilton GR, Baker LA, Rubinstein JL, Kay LE, Benesch JL. The polydispersity of αB-crystallin is rationalized by an interconverting polyhedral architecture. Structure (London, England : 1993). 19: 1855-63. PMID 22153508 DOI: 10.1016/j.str.2011.09.015  1
2011 Kay LE. NMR studies of protein structure and dynamics. 2005. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 213: 477-91. PMID 22152364 DOI: 10.1016/j.jmr.2011.09.009  1
2011 Vallurupalli P, Bouvignies G, Kay LE. Increasing the exchange time-scale that can be probed by CPMG relaxation dispersion NMR. The Journal of Physical Chemistry. B. 115: 14891-900. PMID 22077866 DOI: 10.1021/jp209610v  1
2011 Sun H, Kay LE, Tugarinov V. An optimized relaxation-based coherence transfer NMR experiment for the measurement of side-chain order in methyl-protonated, highly deuterated proteins. The Journal of Physical Chemistry. B. 115: 14878-84. PMID 22040035 DOI: 10.1021/jp209049k  1
2011 Kay LE. NMR studies of protein structure and dynamics - a look backwards and forwards. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 213: 492-4. PMID 21885309 DOI: 10.1016/j.jmr.2011.08.010  1
2011 Bouvignies G, Vallurupalli P, Hansen DF, Correia BE, Lange O, Bah A, Vernon RM, Dahlquist FW, Baker D, Kay LE. Solution structure of a minor and transiently formed state of a T4 lysozyme mutant. Nature. 477: 111-4. PMID 21857680 DOI: 10.1038/nature10349  1
2011 Baldwin AJ, Hilton GR, Lioe H, Bagnéris C, Benesch JL, Kay LE. Quaternary dynamics of αB-crystallin as a direct consequence of localised tertiary fluctuations in the C-terminus. Journal of Molecular Biology. 413: 310-20. PMID 21839749 DOI: 10.1016/j.jmb.2011.07.017  1
2011 Baldwin AJ, Lioe H, Robinson CV, Kay LE, Benesch JL. αB-crystallin polydispersity is a consequence of unbiased quaternary dynamics. Journal of Molecular Biology. 413: 297-309. PMID 21839090 DOI: 10.1016/j.jmb.2011.07.016  1
2011 Kato H, van Ingen H, Zhou BR, Feng H, Bustin M, Kay LE, Bai Y. Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR. Proceedings of the National Academy of Sciences of the United States of America. 108: 12283-8. PMID 21730181 DOI: 10.1073/pnas.1105848108  1
2011 Hansen AL, Kay LE. Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups. Journal of Biomolecular Nmr. 50: 347-55. PMID 21681650 DOI: 10.1007/s10858-011-9520-6  1
2011 Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE. Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study. Journal of the American Chemical Society. 133: 10974-82. PMID 21639149 DOI: 10.1021/ja203686t  1
2011 Ruschak AM, Slassi M, Kay LE, Schimmer AD. Novel proteasome inhibitors to overcome bortezomib resistance. Journal of the National Cancer Institute. 103: 1007-17. PMID 21606441 DOI: 10.1093/jnci/djr160  1
2011 Religa TL, Ruschak AM, Rosenzweig R, Kay LE. Site-directed methyl group labeling as an NMR probe of structure and dynamics in supramolecular protein systems: applications to the proteasome and to the ClpP protease. Journal of the American Chemical Society. 133: 9063-8. PMID 21557628 DOI: 10.1021/ja202259a  1
2011 Hansen DF, Kay LE. Determining valine side-chain rotamer conformations in proteins from methyl 13C chemical shifts: application to the 360 kDa half-proteasome. Journal of the American Chemical Society. 133: 8272-81. PMID 21545099 DOI: 10.1021/ja2014532  1
2011 Kay LE. Solution NMR spectroscopy of supra-molecular systems, why bother? A methyl-TROSY view. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 210: 159-70. PMID 21458338 DOI: 10.1016/j.jmr.2011.03.008  1
2011 Bouvignies G, Vallurupalli P, Cordes MH, Hansen DF, Kay LE. Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy. Journal of Biomolecular Nmr. 50: 13-8. PMID 21424227 DOI: 10.1007/s10858-011-9498-0  1
2011 Dey M, Velyvis A, Li JJ, Chiu E, Chiovitti D, Kay LE, Sicheri F, Dever TE. Requirement for kinase-induced conformational change in eukaryotic initiation factor 2alpha (eIF2alpha) restricts phosphorylation of Ser51. Proceedings of the National Academy of Sciences of the United States of America. 108: 4316-21. PMID 21368187 DOI: 10.1073/pnas.1014872108  1
2011 Bouvignies G, Hansen DF, Vallurupalli P, Kay LE. Divided-evolution-based pulse scheme for quantifying exchange processes in proteins: powerful complement to relaxation dispersion experiments. Journal of the American Chemical Society. 133: 1935-45. PMID 21244030 DOI: 10.1021/ja109589y  1
2010 Kupče Ä’, Kay LE, Freeman R. Detecting the "afterglow" of 13C NMR in proteins using multiple receivers. Journal of the American Chemical Society. 132: 18008-11. PMID 21126087 DOI: 10.1021/ja1080025  1
2010 Ruschak AM, Velyvis A, Kay LE. A simple strategy for ¹³C, ¹H labeling at the Ile-γ2 methyl position in highly deuterated proteins. Journal of Biomolecular Nmr. 48: 129-35. PMID 20949307 DOI: 10.1007/s10858-010-9449-1  1
2010 Ruschak AM, Religa TL, Breuer S, Witt S, Kay LE. The proteasome antechamber maintains substrates in an unfolded state. Nature. 467: 868-71. PMID 20944750 DOI: 10.1038/nature09444  1
2010 Korzhnev DM, Religa TL, Banachewicz W, Fersht AR, Kay LE. A transient and low-populated protein-folding intermediate at atomic resolution. Science (New York, N.Y.). 329: 1312-6. PMID 20829478 DOI: 10.1126/science.1191723  1
2010 Baldwin AJ, Religa TL, Hansen DF, Bouvignies G, Kay LE. 13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics. Journal of the American Chemical Society. 132: 10992-5. PMID 20698653 DOI: 10.1021/ja104578n  1
2010 Li X, Wood TE, Sprangers R, Jansen G, Franke NE, Mao X, Wang X, Zhang Y, Verbrugge SE, Adomat H, Li ZH, Trudel S, Chen C, Religa TL, Jamal N, ... ... Kay LE, et al. Effect of noncompetitive proteasome inhibition on bortezomib resistance. Journal of the National Cancer Institute. 102: 1069-82. PMID 20505154 DOI: 10.1093/jnci/djq198  1
2010 Hansen DF, Neudecker P, Kay LE. Determination of isoleucine side-chain conformations in ground and excited states of proteins from chemical shifts. Journal of the American Chemical Society. 132: 7589-91. PMID 20465253 DOI: 10.1021/ja102090z  1
2010 Bouvignies G, Korzhnev DM, Neudecker P, Hansen DF, Cordes MH, Kay LE. A simple method for measuring signs of (1)H (N) chemical shift differences between ground and excited protein states. Journal of Biomolecular Nmr. 47: 135-41. PMID 20428928 DOI: 10.1007/s10858-010-9418-8  1
2010 Religa TL, Kay LE. Optimal methyl labeling for studies of supra-molecular systems. Journal of Biomolecular Nmr. 47: 163-9. PMID 20422256 DOI: 10.1007/s10858-010-9419-7  1
2010 Religa TL, Sprangers R, Kay LE. Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR. Science (New York, N.Y.). 328: 98-102. PMID 20360109 DOI: 10.1126/science.1184991  1
2010 Stengel F, Baldwin AJ, Painter AJ, Jaya N, Basha E, Kay LE, Vierling E, Robinson CV, Benesch JL. Quaternary dynamics and plasticity underlie small heat shock protein chaperone function. Proceedings of the National Academy of Sciences of the United States of America. 107: 2007-12. PMID 20133845 DOI: 10.1073/pnas.0910126107  1
2010 Auer R, Hansen DF, Neudecker P, Korzhnev DM, Muhandiram DR, Konrat R, Kay LE. Measurement of signs of chemical shift differences between ground and excited protein states: a comparison between H(S/M)QC and R1rho methods. Journal of Biomolecular Nmr. 46: 205-16. PMID 20033258 DOI: 10.1007/s10858-009-9394-z  1
2010 Hansen DF, Neudecker P, Vallurupalli P, Mulder FA, Kay LE. Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion. Journal of the American Chemical Society. 132: 42-3. PMID 20000605 DOI: 10.1021/ja909294n  1
2010 Ruschak AM, Kay LE. Methyl groups as probes of supra-molecular structure, dynamics and function. Journal of Biomolecular Nmr. 46: 75-87. PMID 19784810 DOI: 10.1007/s10858-009-9376-1  1
2010 Mittag T, Kay LE, Forman-Kay JD. Protein dynamics and conformational disorder in molecular recognition. Journal of Molecular Recognition : Jmr. 23: 105-16. PMID 19585546 DOI: 10.1002/jmr.961  1
2009 Lundström P, Vallurupalli P, Hansen DF, Kay LE. Isotope labeling methods for studies of excited protein states by relaxation dispersion NMR spectroscopy. Nature Protocols. 4: 1641-8. PMID 19876024 DOI: 10.1038/nprot.2009.118  1
2009 Velyvis A, Schachman HK, Kay LE. Assignment of Ile, Leu, and Val methyl correlations in supra-molecular systems: an application to aspartate transcarbamoylase. Journal of the American Chemical Society. 131: 16534-43. PMID 19860411 DOI: 10.1021/ja906978r  1
2009 Mittermaier AK, Kay LE. Observing biological dynamics at atomic resolution using NMR. Trends in Biochemical Sciences. 34: 601-11. PMID 19846313 DOI: 10.1016/j.tibs.2009.07.004  1
2009 Hansen DF, Feng H, Zhou Z, Bai Y, Kay LE. Selective characterization of microsecond motions in proteins by NMR relaxation. Journal of the American Chemical Society. 131: 16257-65. PMID 19842628 DOI: 10.1021/ja906842s  1
2009 Baldwin AJ, Kay LE. NMR spectroscopy brings invisible protein states into focus. Nature Chemical Biology. 5: 808-14. PMID 19841630 DOI: 10.1038/nchembio.238  1
2009 Murphy JM, Hansen DF, Wiesner S, Muhandiram DR, Borg M, Smith MJ, Sicheri F, Kay LE, Forman-Kay JD, Pawson T. Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays. Journal of Molecular Biology. 393: 409-24. PMID 19715701 DOI: 10.1016/j.jmb.2009.08.049  1
2009 Hansen DF, Vallurupalli P, Kay LE. Measurement of methyl group motional parameters of invisible, excited protein states by NMR spectroscopy. Journal of the American Chemical Society. 131: 12745-54. PMID 19685870 DOI: 10.1021/ja903897e  1
2009 Baldwin AJ, Hansen DF, Vallurupalli P, Kay LE. Measurement of methyl axis orientations in invisible, excited states of proteins by relaxation dispersion NMR spectroscopy. Journal of the American Chemical Society. 131: 11939-48. PMID 19627152 DOI: 10.1021/ja903896p  1
2009 Auer R, Neudecker P, Muhandiram DR, Lundström P, Hansen DF, Konrat R, Kay LE. Measuring the signs of 1H(alpha) chemical shift differences between ground and excited protein states by off-resonance spin-lock R(1rho) NMR spectroscopy. Journal of the American Chemical Society. 131: 10832-3. PMID 19606858 DOI: 10.1021/ja904315m  1
2009 van Ingen H, Korzhnev DM, Kay LE. An analysis of the effects of 1HN-(1)HN dipolar couplings on the measurement of amide bond vector orientations in invisible protein states by relaxation dispersion NMR. The Journal of Physical Chemistry. B. 113: 9968-77. PMID 19569643 DOI: 10.1021/jp902793y  1
2009 Lundström P, Lin H, Kay LE. Measuring 13Cbeta chemical shifts of invisible excited states in proteins by relaxation dispersion NMR spectroscopy. Journal of Biomolecular Nmr. 44: 139-55. PMID 19448976 DOI: 10.1007/s10858-009-9321-3  1
2009 Hansen DF, Zhou Z, Feng H, Miller Jenkins LM, Bai Y, Kay LE. Binding kinetics of histone chaperone Chz1 and variant histone H2A.Z-H2B by relaxation dispersion NMR spectroscopy. Journal of Molecular Biology. 387: 1-9. PMID 19385041 DOI: 10.1016/j.jmb.2009.01.009  1
2009 Vallurupalli P, Hansen DF, Lundström P, Kay LE. CPMG relaxation dispersion NMR experiments measuring glycine 1H alpha and 13C alpha chemical shifts in the 'invisible' excited states of proteins. Journal of Biomolecular Nmr. 45: 45-55. PMID 19319480 DOI: 10.1007/s10858-009-9310-6  1
2009 Velyvis A, Schachman HK, Kay LE. Application of methyl-TROSY NMR to test allosteric models describing effects of nucleotide binding to aspartate transcarbamoylase. Journal of Molecular Biology. 387: 540-7. PMID 19302799 DOI: 10.1016/j.jmb.2009.01.066  1
2009 Neudecker P, Lundström P, Kay LE. Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding. Biophysical Journal. 96: 2045-54. PMID 19289032 DOI: 10.1016/j.bpj.2008.12.3907  1
2009 Lundström P, Hansen DF, Vallurupalli P, Kay LE. Accurate measurement of alpha proton chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy. Journal of the American Chemical Society. 131: 1915-26. PMID 19152327 DOI: 10.1021/ja807796a  1
2009 Korzhnev DM, Bezsonova I, Lee S, Chalikian TV, Kay LE. Alternate binding modes for a ubiquitin-SH3 domain interaction studied by NMR spectroscopy. Journal of Molecular Biology. 386: 391-405. PMID 19111555 DOI: 10.1016/j.jmb.2008.11.055  1
2009 Mao X, Li X, Sprangers R, Wang X, Venugopal A, Wood T, Zhang Y, Kuntz DA, Coe E, Trudel S, Rose D, Batey RA, Kay LE, Schimmer AD. Clioquinol inhibits the proteasome and displays preclinical activity in leukemia and myeloma. Leukemia. 23: 585-90. PMID 18754030 DOI: 10.1038/leu.2008.232  1
2008 Mittag T, Orlicky S, Choy WY, Tang X, Lin H, Sicheri F, Kay LE, Tyers M, Forman-Kay JD. Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor. Proceedings of the National Academy of Sciences of the United States of America. 105: 17772-7. PMID 19008353 DOI: 10.1073/pnas.0809222105  1
2008 Filippakopoulos P, Kofler M, Hantschel O, Gish GD, Grebien F, Salah E, Neudecker P, Kay LE, Turk BE, Superti-Furga G, Pawson T, Knapp S. Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation. Cell. 134: 793-803. PMID 18775312 DOI: 10.1016/j.cell.2008.07.047  1
2008 Lundström P, Hansen DF, Kay LE. Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively (13)C labeled samples. Journal of Biomolecular Nmr. 42: 35-47. PMID 18762869 DOI: 10.1007/s10858-008-9260-4  1
2008 Vallurupalli P, Hansen DF, Kay LE. Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 105: 11766-71. PMID 18701719 DOI: 10.1073/pnas.0804221105  1
2008 Zhou Z, Feng H, Hansen DF, Kato H, Luk E, Freedberg DI, Kay LE, Wu C, Bai Y. NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B. Nature Structural & Molecular Biology. 15: 868-9. PMID 18641662 DOI: 10.1038/nsmb.1465  1
2008 Hansen DF, Vallurupalli P, Kay LE. Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states. Journal of Biomolecular Nmr. 41: 113-20. PMID 18574698 DOI: 10.1007/s10858-008-9251-5  1
2008 Sprangers R, Li X, Mao X, Rubinstein JL, Schimmer AD, Kay LE. TROSY-based NMR evidence for a novel class of 20S proteasome inhibitors. Biochemistry. 47: 6727-34. PMID 18540636 DOI: 10.1021/bi8005913  1
2008 Hass MA, Hansen DF, Christensen HE, Led JJ, Kay LE. Characterization of conformational exchange of a histidine side chain: protonation, rotamerization, and tautomerization of His61 in plastocyanin from Anabaena variabilis. Journal of the American Chemical Society. 130: 8460-70. PMID 18540585 DOI: 10.1021/ja801330h  1
2008 Hansen DF, Vallurupalli P, Kay LE. Quantifying two-bond 1HN-13CO and one-bond 1H(alpha)-13C(alpha) dipolar couplings of invisible protein states by spin-state selective relaxation dispersion NMR spectroscopy. Journal of the American Chemical Society. 130: 8397-405. PMID 18528998 DOI: 10.1021/ja801005n  1
2008 Korzhnev DM, Kay LE. Probing invisible, low-populated States of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding. Accounts of Chemical Research. 41: 442-51. PMID 18275162 DOI: 10.1021/ar700189y  1
2008 Vallurupalli P, Hansen DF, Kay LE. Probing structure in invisible protein states with anisotropic NMR chemical shifts. Journal of the American Chemical Society. 130: 2734-5. PMID 18257570 DOI: 10.1021/ja710817g  1
2008 Hansen DF, Vallurupalli P, Lundström P, Neudecker P, Kay LE. Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy: how well can we do? Journal of the American Chemical Society. 130: 2667-75. PMID 18237174 DOI: 10.1021/ja078337p  1
2008 Grishaev A, Tugarinov V, Kay LE, Trewhella J, Bax A. Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints. Journal of Biomolecular Nmr. 40: 95-106. PMID 18008171 DOI: 10.1007/s10858-007-9211-5  0.52
2008 Hansen DF, Vallurupalli P, Kay LE. An improved 15N relaxation dispersion experiment for the measurement of millisecond time-scale dynamics in proteins. The Journal of Physical Chemistry. B. 112: 5898-904. PMID 18001083 DOI: 10.1021/jp074793o  1
2007 Vallurupalli P, Hansen DF, Stollar E, Meirovitch E, Kay LE. Measurement of bond vector orientations in invisible excited states of proteins. Proceedings of the National Academy of Sciences of the United States of America. 104: 18473-7. PMID 18006656 DOI: 10.1073/pnas.0708296104  1
2007 Sprangers R, Kay LE. Probing supramolecular structure from measurement of methyl (1)H-(13)C residual dipolar couplings. Journal of the American Chemical Society. 129: 12668-9. PMID 17910459 DOI: 10.1021/ja075846i  1
2007 Neudecker P, Zarrine-Afsar A, Davidson AR, Kay LE. Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 104: 15717-22. PMID 17898173 DOI: 10.1073/pnas.0705097104  1
2007 Sprangers R, Velyvis A, Kay LE. Solution NMR of supramolecular complexes: providing new insights into function. Nature Methods. 4: 697-703. PMID 17762877 DOI: 10.1038/nmeth1080  1
2007 Murphy JM, Korzhnev DM, Ceccarelli DF, Briant DJ, Zarrine-Afsar A, Sicheri F, Kay LE, Pawson T. Conformational instability of the MARK3 UBA domain compromises ubiquitin recognition and promotes interaction with the adjacent kinase domain. Proceedings of the National Academy of Sciences of the United States of America. 104: 14336-41. PMID 17726107 DOI: 10.1073/pnas.0703012104  1
2007 Hansen DF, Yang D, Feng H, Zhou Z, Wiesner S, Bai Y, Kay LE. An exchange-free measure of 15N transverse relaxation: an NMR spectroscopy application to the study of a folding intermediate with pervasive chemical exchange. Journal of the American Chemical Society. 129: 11468-79. PMID 17722922 DOI: 10.1021/ja072717t  1
2007 Korzhnev DM, Religa TL, Lundström P, Fersht AR, Kay LE. The folding pathway of an FF domain: characterization of an on-pathway intermediate state under folding conditions by (15)N, (13)C(alpha) and (13)C-methyl relaxation dispersion and (1)H/(2)H-exchange NMR spectroscopy. Journal of Molecular Biology. 372: 497-512. PMID 17689561 DOI: 10.1016/j.jmb.2007.06.012  1
2007 Tugarinov V, Kay LE. Separating degenerate (1)H transitions in methyl group probes for single-quantum (1)H-CPMG relaxation dispersion NMR spectroscopy. Journal of the American Chemical Society. 129: 9514-21. PMID 17628064 DOI: 10.1021/ja0726456  1
2007 Lundström P, Teilum K, Carstensen T, Bezsonova I, Wiesner S, Hansen DF, Religa TL, Akke M, Kay LE. Fractional 13C enrichment of isolated carbons using [1-13C]- or [2- 13C]-glucose facilitates the accurate measurement of dynamics at backbone Calpha and side-chain methyl positions in proteins. Journal of Biomolecular Nmr. 38: 199-212. PMID 17554498 DOI: 10.1007/s10858-007-9158-6  1
2007 Velyvis A, Yang YR, Schachman HK, Kay LE. A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase. Proceedings of the National Academy of Sciences of the United States of America. 104: 8815-20. PMID 17502625 DOI: 10.1073/pnas.0703347104  1
2007 Lundström P, Vallurupalli P, Religa TL, Dahlquist FW, Kay LE. A single-quantum methyl 13C-relaxation dispersion experiment with improved sensitivity. Journal of Biomolecular Nmr. 38: 79-88. PMID 17464570 DOI: 10.1007/s10858-007-9149-7  1
2007 Vallurupalli P, Scott L, Williamson JR, Kay LE. Strong coupling effects during X-pulse CPMG experiments recorded on heteronuclear ABX spin systems: artifacts and a simple solution. Journal of Biomolecular Nmr. 38: 41-6. PMID 17334825 DOI: 10.1007/s10858-006-9139-1  1
2007 Hansen DF, Kay LE. Improved magnetization alignment schemes for spin-lock relaxation experiments. Journal of Biomolecular Nmr. 37: 245-55. PMID 17310328 DOI: 10.1007/s10858-006-9126-6  1
2007 Zhuravleva A, Korzhnev DM, Nolde SB, Kay LE, Arseniev AS, Billeter M, Orekhov VY. Propagation of dynamic changes in barnase upon binding of barstar: an NMR and computational study. Journal of Molecular Biology. 367: 1079-92. PMID 17306298 DOI: 10.1016/j.jmb.2007.01.051  1
2007 Tugarinov V, Sprangers R, Kay LE. Probing side-chain dynamics in the proteasome by relaxation violated coherence transfer NMR spectroscopy. Journal of the American Chemical Society. 129: 1743-50. PMID 17249677 DOI: 10.1021/ja067827z  1
2007 Sprangers R, Kay LE. Quantitative dynamics and binding studies of the 20S proteasome by NMR. Nature. 445: 618-22. PMID 17237764 DOI: 10.1038/nature05512  1
2006 Tugarinov V, Kanelis V, Kay LE. Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy. Nature Protocols. 1: 749-54. PMID 17406304 DOI: 10.1038/nprot.2006.101  1
2006 Neudecker P, Zarrine-Afsar A, Choy WY, Muhandiram DR, Davidson AR, Kay LE. Identification of a collapsed intermediate with non-native long-range interactions on the folding pathway of a pair of Fyn SH3 domain mutants by NMR relaxation dispersion spectroscopy. Journal of Molecular Biology. 363: 958-76. PMID 16989862 DOI: 10.1016/j.jmb.2006.08.047  1
2006 Tugarinov V, Kay LE. A 2H NMR relaxation experiment for the measurement of the time scale of methyl side-chain dynamics in large proteins. Journal of the American Chemical Society. 128: 12484-9. PMID 16984199 DOI: 10.1021/ja063071s  1
2006 Korzhnev DM, Neudecker P, Zarrine-Afsar A, Davidson AR, Kay LE. Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states. Biochemistry. 45: 10175-83. PMID 16922492 DOI: 10.1021/bi0611560  1
2006 Vallurupalli P, Kay LE. Complementarity of ensemble and single-molecule measures of protein motion: a relaxation dispersion NMR study of an enzyme complex. Proceedings of the National Academy of Sciences of the United States of America. 103: 11910-5. PMID 16880391 DOI: 10.1073/pnas.0602310103  1
2006 Vallurupalli P, Scott L, Hennig M, Williamson JR, Kay LE. New RNA labeling methods offer dramatic sensitivity enhancements in 2H NMR relaxation spectra. Journal of the American Chemical Society. 128: 9346-7. PMID 16848466 DOI: 10.1021/ja0632512  1
2006 Tugarinov V, Ollerenshaw JE, Kay LE. Dipolar dynamic frequency shifts in multiple-quantum spectra of methyl groups in proteins: correlation with side-chain motion. Magnetic Resonance in Chemistry : Mrc. 44: S122-9. PMID 16826549 DOI: 10.1002/mrc.1819  1
2006 Evanics F, Hwang PM, Cheng Y, Kay LE, Prosser RS. Topology of an outer-membrane enzyme: Measuring oxygen and water contacts in solution NMR studies of PagP. Journal of the American Chemical Society. 128: 8256-64. PMID 16787090 DOI: 10.1021/ja0610075  1
2006 Tugarinov V, Kay LE. Relaxation rates of degenerate 1H transitions in methyl groups of proteins as reporters of side-chain dynamics. Journal of the American Chemical Society. 128: 7299-308. PMID 16734484 DOI: 10.1021/ja060817d  1
2006 Tollinger M, Neale C, Kay LE, Forman-Kay JD. Characterization of the hydrodynamic properties of the folding transition state of an SH3 domain by magnetization transfer NMR spectroscopy. Biochemistry. 45: 6434-45. PMID 16700554 DOI: 10.1021/bi060268o  1
2006 Brath U, Akke M, Yang D, Kay LE, Mulder FA. Functional dynamics of human FKBP12 revealed by methyl 13C rotating frame relaxation dispersion NMR spectroscopy. Journal of the American Chemical Society. 128: 5718-27. PMID 16637639 DOI: 10.1021/ja0570279  1
2006 Mittermaier A, Kay LE. New tools provide new insights in NMR studies of protein dynamics. Science (New York, N.Y.). 312: 224-8. PMID 16614210 DOI: 10.1126/science.1124964  1
2006 Korzhnev DM, Bezsonova I, Evanics F, Taulier N, Zhou Z, Bai Y, Chalikian TV, Prosser RS, Kay LE. Probing the transition state ensemble of a protein folding reaction by pressure-dependent NMR relaxation dispersion. Journal of the American Chemical Society. 128: 5262-9. PMID 16608362 DOI: 10.1021/ja0601540  1
2006 Bezsonova I, Korzhnev DM, Prosser RS, Forman-Kay JD, Kay LE. Hydration and packing along the folding pathway of SH3 domains by pressure-dependent NMR. Biochemistry. 45: 4711-9. PMID 16605239 DOI: 10.1021/bi060177r  1
2006 Neudecker P, Korzhnev DM, Kay LE. Assessment of the effects of increased relaxation dispersion data on the extraction of 3-site exchange parameters characterizing the unfolding of an SH3 domain. Journal of Biomolecular Nmr. 34: 129-35. PMID 16604422 DOI: 10.1007/s10858-006-0001-2  1
2006 Zarrine-Afsar A, Mittermaier A, Kay LE, Davidson AR. Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain. Protein Science : a Publication of the Protein Society. 15: 162-70. PMID 16373478 DOI: 10.1110/ps.051829106  1
2005 Graves, Pufall, Nelson ML, Lee GM, Kang HS, McIntosh LP, Velyvis A, Kay LE. Regulating ETS transcription factor function by altering a flexible domain Cancer Biology and Therapy. 4. PMID 16710935  1
2005 Tugarinov V, Kay LE. Quantitative 13C and 2H NMR relaxation studies of the 723-residue enzyme malate synthase G reveal a dynamic binding interface. Biochemistry. 44: 15970-7. PMID 16331956 DOI: 10.1021/bi0519809  1
2005 Mittermaier A, Korzhnev DM, Kay LE. Side-chain interactions in the folding pathway of a Fyn SH3 domain mutant studied by relaxation dispersion NMR spectroscopy. Biochemistry. 44: 15430-6. PMID 16300390 DOI: 10.1021/bi051771o  1
2005 Eisenmesser EZ, Millet O, Labeikovsky W, Korzhnev DM, Wolf-Watz M, Bosco DA, Skalicky JJ, Kay LE, Kern D. Intrinsic dynamics of an enzyme underlies catalysis. Nature. 438: 117-21. PMID 16267559 DOI: 10.1038/nature04105  1
2005 Sprangers R, Gribun A, Hwang PM, Houry WA, Kay LE. Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release. Proceedings of the National Academy of Sciences of the United States of America. 102: 16678-83. PMID 16263929 DOI: 10.1073/pnas.0507370102  1
2005 Korzhnev DM, Neudecker P, Mittermaier A, Orekhov VY, Kay LE. Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: an application to the folding of a Fyn SH3 domain mutant. Journal of the American Chemical Society. 127: 15602-11. PMID 16262426 DOI: 10.1021/ja054550e  1
2005 Ollerenshaw JE, Tugarinov V, Skrynnikov NR, Kay LE. Comparison of 13CH3, 13CH2D, and 13CHD2 methyl labeling strategies in proteins. Journal of Biomolecular Nmr. 33: 25-41. PMID 16222555 DOI: 10.1007/s10858-005-2614-2  1
2005 Tugarinov V, Kay LE. Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteins. Chembiochem : a European Journal of Chemical Biology. 6: 1567-77. PMID 16075427 DOI: 10.1002/cbic.200500110  1
2005 Pufall MA, Lee GM, Nelson ML, Kang HS, Velyvis A, Kay LE, McIntosh LP, Graves BJ. Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region. Science (New York, N.Y.). 309: 142-5. PMID 15994560 DOI: 10.1126/science.1111915  1
2005 Tollinger M, Kay LE, Forman-Kay JD. Measuring pK(a) values in protein folding transition state ensembles by NMR spectroscopy. Journal of the American Chemical Society. 127: 8904-5. PMID 15969539 DOI: 10.1021/ja051942c  1
2005 Korzhnev DM, Mittermaier AK, Kay LE. Cross-correlated spin relaxation effects in methyl 1H CPMG-based relaxation dispersion experiments: complications and a simple solution. Journal of Biomolecular Nmr. 31: 337-42. PMID 15929000 DOI: 10.1007/s10858-005-2468-7  1
2005 Tugarinov V, Ollerenshaw JE, Kay LE. Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme. Journal of the American Chemical Society. 127: 8214-25. PMID 15926851 DOI: 10.1021/ja0508830  1
2005 Vallurupalli P, Kay LE. A suite of 2H NMR spin relaxation experiments for the measurement of RNA dynamics. Journal of the American Chemical Society. 127: 6893-901. PMID 15869313 DOI: 10.1021/ja0427799  1
2005 Choy WY, Zhou Z, Bai Y, Kay LE. An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mutants of apocytochrome b562. Journal of the American Chemical Society. 127: 5066-72. PMID 15810841 DOI: 10.1021/ja042560u  1
2005 Hwang PM, Kay LE. Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP. Methods in Enzymology. 394: 335-50. PMID 15808227 DOI: 10.1016/S0076-6879(05)94013-5  1
2005 Kay LE. NMR studies of protein structure and dynamics. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 173: 193-207. PMID 15780912 DOI: 10.1016/j.jmr.2004.11.021  1
2005 Xu J, Millet O, Kay LE, Skrynnikov NR. A new spin probe of protein dynamics: nitrogen relaxation in 15N-2H amide groups. Journal of the American Chemical Society. 127: 3220-9. PMID 15740163 DOI: 10.1021/ja040215z  1
2005 Tugarinov V, Kay LE, Ibraghimov I, Orekhov VY. High-resolution four-dimensional 1H-13C NOE spectroscopy using methyl-TROSY, sparse data acquisition, and multidimensional decomposition. Journal of the American Chemical Society. 127: 2767-75. PMID 15725035 DOI: 10.1021/ja044032o  1
2005 Korzhnev DM, Orekhov VY, Kay LE. Off-resonance R(1rho) NMR studies of exchange dynamics in proteins with low spin-lock fields: an application to a Fyn SH3 domain. Journal of the American Chemical Society. 127: 713-21. PMID 15643897 DOI: 10.1021/ja0446855  1
2005 Finerty PJ, Mittermaier AK, Muhandiram R, Kay LE, Forman-Kay JD. NMR dynamics-derived insights into the binding properties of a peptide interacting with an SH2 domain. Biochemistry. 44: 694-703. PMID 15641795 DOI: 10.1021/bi048641k  1
2005 Tugarinov V, Choy WY, Orekhov VY, Kay LE. Solution NMR-derived global fold of a monomeric 82-kDa enzyme. Proceedings of the National Academy of Sciences of the United States of America. 102: 622-7. PMID 15637152 DOI: 10.1073/pnas.0407792102  1
2004 Tugarinov V, Choy WY, Kupce E, Kay LE. Addressing the overlap problem in the quantitative analysis of two dimensional NMR spectra: application to (15)N relaxation measurements. Journal of Biomolecular Nmr. 30: 347-52. PMID 15756461 DOI: 10.1007/s10858-005-1549-y  1
2004 Tugarinov V, Scheurer C, Brüschweiler R, Kay LE. Estimates of methyl 13C and 1H CSA values (Deltasigma) in proteins from cross-correlated spin relaxation. Journal of Biomolecular Nmr. 30: 397-406. PMID 15630560 DOI: 10.1007/s10858-004-4349-x  1
2004 Ollerenshaw JE, Kaya H, Chan HS, Kay LE. Sparsely populated folding intermediates of the Fyn SH3 domain: matching native-centric essential dynamics and experiment. Proceedings of the National Academy of Sciences of the United States of America. 101: 14748-53. PMID 15469926 DOI: 10.1073/pnas.0404436101  1
2004 Tugarinov V, Kay LE. Stereospecific NMR assignments of prochiral methyls, rotameric states and dynamics of valine residues in malate synthase G. Journal of the American Chemical Society. 126: 9827-36. PMID 15291587 DOI: 10.1021/ja048738u  1
2004 Korzhnev DM, Salvatella X, Vendruscolo M, Di Nardo AA, Davidson AR, Dobson CM, Kay LE. Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR. Nature. 430: 586-90. PMID 15282609 DOI: 10.1038/nature02655  1
2004 Ahn VE, Lo EI, Engel CK, Chen L, Hwang PM, Kay LE, Bishop RE, Privé GG. A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin. The Embo Journal. 23: 2931-41. PMID 15272304 DOI: 10.1038/sj.emboj.7600320  0.52
2004 Tugarinov V, Kay LE. 1H,13C-1H,1H dipolar cross-correlated spin relaxation in methyl groups. Journal of Biomolecular Nmr. 29: 369-76. PMID 15213435 DOI: 10.1023/B:JNMR.0000032562.07475.7f  1
2004 Hwang PM, Bishop RE, Kay LE. The integral membrane enzyme PagP alternates between two dynamically distinct states. Proceedings of the National Academy of Sciences of the United States of America. 101: 9618-23. PMID 15210985 DOI: 10.1073/pnas.0402324101  1
2004 Tugarinov V, Hwang PM, Kay LE. Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins. Annual Review of Biochemistry. 73: 107-46. PMID 15189138 DOI: 10.1146/annurev.biochem.73.011303.074004  1
2004 Korzhnev DM, Kloiber K, Kay LE. Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: theory and application. Journal of the American Chemical Society. 126: 7320-9. PMID 15186169 DOI: 10.1021/ja049968b  1
2004 Di Nardo AA, Korzhnev DM, Stogios PJ, Zarrine-Afsar A, Kay LE, Davidson AR. Dramatic acceleration of protein folding by stabilization of a nonnative backbone conformation. Proceedings of the National Academy of Sciences of the United States of America. 101: 7954-9. PMID 15148398 DOI: 10.1073/pnas.0400550101  1
2004 Tugarinov V, Sprangers R, Kay LE. Line narrowing in methyl-TROSY using zero-quantum 1H-13C NMR spectroscopy. Journal of the American Chemical Society. 126: 4921-5. PMID 15080697 DOI: 10.1021/ja039732s  1
2004 Mittermaier A, Kay LE. The response of internal dynamics to hydrophobic core mutations in the SH3 domain from the Fyn tyrosine kinase. Protein Science : a Publication of the Protein Society. 13: 1088-99. PMID 15044737 DOI: 10.1110/ps.03502504  1
2004 Korzhnev DM, Kloiber K, Kanelis V, Tugarinov V, Kay LE. Probing Slow Dynamics in High Molecular Weight Proteins by Methyl-TROSY NMR Spectroscopy: Application to a 723-Residue Enzyme Journal of the American Chemical Society. 126: 3964-3973. PMID 15038751 DOI: 10.1021/ja039587i  1
2004 Orekhov VY, Korzhnev DM, Kay LE. Double- and Zero-Quantum NMR Relaxation Dispersion Experiments Sampling Millisecond Time Scale Dynamics in Proteins Journal of the American Chemical Society. 126: 1886-1891. PMID 14871121  1
2004 Tugarinov V, Kay LE. An isotope labeling strategy for methyl TROSY spectroscopy Journal of Biomolecular Nmr. 28: 165-172. PMID 14755160 DOI: 10.1023/B:JNMR.0000013824.93994.1f  1
2003 Tugarinov V, Kay LE. Ile, Leu, and Val Methyl Assignments of the 723-Residue Malate Synthase G Using a New Labeling Strategy and Novel NMR Methods Journal of the American Chemical Society. 125: 13868-13878. PMID 14599227 DOI: 10.1021/ja030345s  1
2003 Millet O, Hudson RP, Kay LE. The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fluorescence spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 100: 12700-5. PMID 14530390 DOI: 10.1073/pnas.2134311100  1
2003 Kupce E, Muhandiram DR, Kay LE. A combined HNCA/HNCO experiment for 15N labeled proteins with 13C at natural abundance Journal of Biomolecular Nmr. 27: 175-179. PMID 12913414 DOI: 10.1023/A:1024985219764  1
2003 Ollerenshaw JE, Lidar DA, Kay LE. Magnetic resonance realization of decoherence-free quantum computation Physical Review Letters. 91: 217904/1-217904/4.  1
2002 Mal TK, Skrynnikov NR, Yap KL, Kay LE, Ikura M. Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR. Biochemistry. 41: 12899-906. PMID 12390014 DOI: 10.1021/bi0264162  1
2002 Skrynnikov NR, Dahlquist FW, Kay LE. Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments. Journal of the American Chemical Society. 124: 12352-60. PMID 12371879 DOI: 10.1021/ja0207089  1
2002 Korzhnev DM, Skrynnikov NR, Millet O, Torchia DA, Kay LE. An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates. Journal of the American Chemical Society. 124: 10743-53. PMID 12207529 DOI: 10.1021/ja0204776  1
2002 Skrynnikov NR, Millet O, Kay LE. Deuterium spin probes of side-chain dynamics in proteins. 2. Spectral density mapping and identification of nanosecond time-scale side-chain motions. Journal of the American Chemical Society. 124: 6449-60. PMID 12033876 DOI: 10.1021/ja012498q  1
2002 Millet O, Muhandiram DR, Skrynnikov NR, Kay LE. Deuterium spin probes of side-chain dynamics in proteins. 1. Measurement of five relaxation rates per deuteron in (13)C-labeled and fractionally (2)H-enriched proteins in solution. Journal of the American Chemical Society. 124: 6439-48. PMID 12033875 DOI: 10.1021/ja012497y  1
2001 Tollinger M, Skrynnikov NR, Mulder FA, Forman-Kay JD, Kay LE. Slow dynamics in folded and unfolded states of an SH3 domain. Journal of the American Chemical Society. 123: 11341-52. PMID 11707108 DOI: 10.1021/ja011300z  1
2001 Donaldson LW, Skrynnikov NR, Choy WY, Muhandiram DR, Sarkar B, Forman-Kay JD, Kay LE. Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy. Journal of the American Chemical Society. 123: 9843-7. PMID 11583547 DOI: 10.1021/ja011241p  1
2001 Skrynnikov NR, Mulder FA, Hon B, Dahlquist FW, Kay LE. Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: application to methionine residues in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society. 123: 4556-66. PMID 11457242 DOI: 10.1021/ja004179p  1
2001 Tolman JR, Al-Hashimi HM, Kay LE, Prestegard JH. Structural and dynamic analysis of residual dipolar coupling data for proteins. Journal of the American Chemical Society. 123: 1416-24. PMID 11456715 DOI: 10.1021/ja002500y  1
2001 Mulder FA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE. Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society. 123: 967-75. PMID 11456632 DOI: 10.1021/ja003447g  1
2001 Hwang PM, Skrynnikov NR, Kay LE. Domain orientation in beta-cyclodextrin-loaded maltose binding protein: diffusion anisotropy measurements confirm the results of a dipolar coupling study. Journal of Biomolecular Nmr. 20: 83-8. PMID 11430759 DOI: 10.1023/A:1011226512421  1
2001 Evenäs J, Tugarinov V, Skrynnikov NR, Goto NK, Muhandiram R, Kay LE. Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy. Journal of Molecular Biology. 309: 961-74. PMID 11399072 DOI: 10.1006/jmbi.2001.4695  1
2001 Goto NK, Skrynnikov NR, Dahlquist FW, Kay LE. What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR. Journal of Molecular Biology. 308: 745-64. PMID 11350172 DOI: 10.1006/jmbi.2001.4614  1
2000 Skrynnikov NR, Kay LE. Assessment of molecular structure using frame-independent orientational restraints derived from residual dipolar couplings. Journal of Biomolecular Nmr. 18: 239-52. PMID 11142514  1
2000 Mueller GA, Choy WY, Skrynnikov NR, Kay LE. A method for incorporating dipolar couplings into structure calculations in cases of (near) axial symmetry of alignment. Journal of Biomolecular Nmr. 18: 183-8. PMID 11142508  1
2000 Goto NK, Kay LE. New developments in isotope labeling strategies for protein solution NMR spectroscopy. Current Opinion in Structural Biology. 10: 585-92. PMID 11042458 DOI: 10.1016/S0959-440X(00)00135-4  1
2000 Skrynnikov NR, Goto NK, Yang D, Choy WY, Tolman JR, Mueller GA, Kay LE. Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin. Journal of Molecular Biology. 295: 1265-73. PMID 10653702 DOI: 10.1006/jmbi.1999.3430  1
1999 Goto NK, Gardner KH, Mueller GA, Willis RC, Kay LE. A robust and cost-effective method for the production of Val, Leu, Ile (delta 1) methyl-protonated 15N-, 13C-, 2H-labeled proteins. Journal of Biomolecular Nmr. 13: 369-74. PMID 10383198 DOI: 10.1023/A:1008393201236  1
1998 Yang D, Tolman JR, Goto NK, Kay LE. An HNCO-based Pulse Scheme for the Measurement of 13Cα-1Hα One-bond Dipolar couplings in 15N, 13C Labeled Proteins. Journal of Biomolecular Nmr. 12: 325-32. PMID 21136327 DOI: 10.1023/A:1008223017233  1
1998 Yang D, Gardner KH, Kay LE. A Sensitive Pulse Scheme for Measuring the Backbone Dihedral Angle psi Based on Cross-correlation Between (13)C (alpha)- (1)Halpha Dipolar and Carbonyl Chemical Shift Anisotropy Relaxation Interactions. Journal of Biomolecular Nmr. 11: 213-20. PMID 20700829 DOI: 10.1023/A:1008284315816  1
1998 Shan X, Gardner KH, Muhandiram DR, Kay LE, Arrowsmith CH. Subunit-specific backbone NMR assignments of a 64 kDa trp repressor/DNA complex: a role for N-terminal residues in tandem binding. Journal of Biomolecular Nmr. 11: 307-18. PMID 9691278  1
1998 Gardner KH, Kay LE. The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins. Annual Review of Biophysics and Biomolecular Structure. 27: 357-406. PMID 9646872 DOI: 10.1146/annurev.biophys.27.1.357  1
1997 Kay LE, Gardner KH. Solution NMR spectroscopy beyond 25 kDa. Current Opinion in Structural Biology. 7: 722-31. PMID 9345633 DOI: 10.1016/S0959-440X(97)80084-X  1
1997 Gardner KH, Rosen MK, Kay LE. Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR. Biochemistry. 36: 1389-401. PMID 9063887 DOI: 10.1021/bi9624806  1
1996 Gardner KH, Konrat R, Rosen MK, Kay LE. An (H)C(CO)NH-TOCSY pulse scheme for sequential assignment of protonated methyl groups in otherwise deuterated (15)N, (13)C-labeled proteins. Journal of Biomolecular Nmr. 8: 351-6. PMID 20686885 DOI: 10.1007/BF00410333  1
1996 Rosen MK, Gardner KH, Willis RC, Parris WE, Pawson T, Kay LE. Selective methyl group protonation of perdeuterated proteins. Journal of Molecular Biology. 263: 627-36. PMID 8947563 DOI: 10.1006/jmbi.1996.0603  1
1992 Nicholson LK, Kay LE, Baldisseri DM, Arango J, Young PE, Bax A, Torchia DA. Dynamics of methyl groups in proteins as studied by proton-detected 13C NMR spectroscopy. Application to the leucine residues of staphylococcal nuclease. Biochemistry. 31: 5253-63. PMID 1606149  1
1989 Kay LE, Torchia DA, Bax A. Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry. 28: 8972-9. PMID 2690953  1
1988 Frederick AF, Kay LE, Prestegard JH. Location of divalent ion sites in acyl carrier protein using relaxation perturbed 2D NMR. Febs Letters. 238: 43-8. PMID 3049158 DOI: 10.1016/0014-5793(88)80222-9  1
1988 LeMaster DM, Kay LE, Brünger AT, Prestegard JH. Protein dynamics and distance determination by NOE measurements. Febs Letters. 236: 71-6. PMID 2841170 DOI: 10.1016/0014-5793(88)80287-4  1
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