Year |
Citation |
Score |
2023 |
Yang Y, Feng RR, Gai F. 4-Cyanotryptophan as a Sensitive Fluorescence Probe of Local Electric Field of Proteins. The Journal of Physical Chemistry. B. 127: 514-519. PMID 36598839 DOI: 10.1021/acs.jpcb.2c07605 |
0.303 |
|
2020 |
Acharyya A, Ahmed IA, Gai F. 4-Cyanoindole-based fluorophores for biological spectroscopy and microscopy. Methods in Enzymology. 639: 191-215. PMID 32475401 DOI: 10.1016/Bs.Mie.2020.04.014 |
0.34 |
|
2020 |
Acharyya A, Shin D, Troxler T, Gai F. Can glycine betaine denature proteins? Physical Chemistry Chemical Physics : Pccp. PMID 32242578 DOI: 10.1039/D0Cp00397B |
0.399 |
|
2019 |
Ahmed IA, Rodgers JM, Eng C, Troxler T, Gai F. PET and FRET utility of an amino acid pair: tryptophan and 4-cyanotryptophan. Physical Chemistry Chemical Physics : Pccp. PMID 31179453 DOI: 10.1039/C9Cp02126D |
0.324 |
|
2019 |
Abaskharon RM, Mukherjee D, Gai F. 4-Oxoproline as a Site-Specific Infrared Probe: Application to Assess Proline Isomerization and Dimer Formation. The Journal of Physical Chemistry. B. PMID 31135160 DOI: 10.1021/Acs.Jpcb.9B03766 |
0.363 |
|
2019 |
Zhang K, Ahmed IA, Kratochvil HT, DeGrado WF, Gai F, Jo H. Synthesis and application of the blue fluorescent amino acid l-4-cyanotryptophan to assess peptide-membrane interactions. Chemical Communications (Cambridge, England). PMID 30957824 DOI: 10.1039/C9Cc01152H |
0.346 |
|
2019 |
Ahmed IA, Acharyya A, Eng CM, Rodgers JM, DeGrado WF, Jo H, Gai F. 4-Cyanoindole-2'-deoxyribonucleoside as a Dual Fluorescence and Infrared Probe of DNA Structure and Dynamics. Molecules (Basel, Switzerland). 24. PMID 30744004 DOI: 10.3390/Molecules24030602 |
0.353 |
|
2019 |
Acharyya A, Ge Y, Wu H, DeGrado WF, Voelz VA, Gai F. Exposing the Nucleation Site in α-Helix Folding: A Joint Experimental and Simulation Study. The Journal of Physical Chemistry. B. PMID 30694671 DOI: 10.1021/Acs.Jpcb.8B12220 |
0.413 |
|
2019 |
Fong KPY, Ahmed IA, Mravic M, Jo H, DeGrado WF, Gai F, Bennett JS. Direct Visualization of Platelet Integrins Using ANTI-Transmembrane Domain Peptides Containing a BLUE Fluorescent Amino Acid Blood. 134: 2344-2344. DOI: 10.1182/Blood-2019-128363 |
0.316 |
|
2018 |
Pazos IM, Ma J, Mukherjee D, Gai F. Ultrafast Hydrogen-Bonding Dynamics in Amyloid Fibrils. The Journal of Physical Chemistry. B. PMID 29883122 DOI: 10.1021/Acs.Jpcb.8B04642 |
0.345 |
|
2018 |
Dollé JP, Rodgers JM, Browne KD, Troxler T, Gai F, Smith DH. Newfound effect of N-acetylaspartate in preventing and reversing aggregation of amyloid-beta in vitro. Neurobiology of Disease. PMID 29859874 DOI: 10.1016/J.Nbd.2018.05.023 |
0.319 |
|
2018 |
Ding B, Yang L, Mukherjee D, Chen J, Gao YQ, Gai F. Microscopic Insight into the Protein Denaturation Action of Urea and Its Methyl Derivatives. The Journal of Physical Chemistry Letters. PMID 29767523 DOI: 10.1021/Acs.Jpclett.8B00960 |
0.679 |
|
2018 |
Wu H, Acharyya A, Wu Y, Liu L, Jo H, Gai F, DeGrado W. Design of a short thermally stable α-helix embedded in a macrocycle. Chembiochem : a European Journal of Chemical Biology. PMID 29417711 DOI: 10.1002/Cbic.201800026 |
0.446 |
|
2018 |
Mukherjee D, Ortiz Rodriguez LI, Hilaire MR, Troxler T, Gai F. 7-Cyanoindole fluorescence as a local hydration reporter: application to probe the microheterogeneity of nine water-organic binary mixtures. Physical Chemistry Chemical Physics : Pccp. PMID 29313858 DOI: 10.1039/C7Cp07160D |
0.333 |
|
2018 |
Kratochvil HT, Thomaston JL, Gai F, DeGrado WF. Proton Stabilization and Conduction Pathway in the Matrix Protein M2 Biophysical Journal. 114: 240a-241a. DOI: 10.1016/J.Bpj.2017.11.1339 |
0.305 |
|
2017 |
Hilaire MR, Ding B, Mukherjee D, Chen J, Gai F. Possible Existence of α-Sheets in the Amyloid Fibrils Formed by a TTR105-115 Mutant. Journal of the American Chemical Society. PMID 29241000 DOI: 10.1021/Jacs.7B09262 |
0.644 |
|
2017 |
Hilaire MR, Mukherjee D, Troxler T, Gai F. Solvent Dependence of Cyanoindole Fluorescence Lifetime. Chemical Physics Letters. 685: 133-138. PMID 29225366 DOI: 10.1016/J.Cplett.2017.07.038 |
0.334 |
|
2017 |
Abaskharon RM, Brown SP, Zhang W, Chen J, Smith AB, Gai F. Isotope-Labeled Aspartate Sidechain as a Non-Perturbing Infrared Probe: Application to Investigate the Dynamics of a Carboxylate Buried Inside a Protein. Chemical Physics Letters. 683: 193-198. PMID 29033461 DOI: 10.1016/J.Cplett.2017.03.064 |
0.377 |
|
2017 |
Stöhr J, Wu H, Nick M, Wu Y, Bhate M, Condello C, Johnson N, Rodgers J, Lemmin T, Acharya S, Becker J, Robinson K, Kelly MJS, Gai F, Stubbs G, et al. A 31-residue peptide induces aggregation of tau's microtubule-binding region in cells. Nature Chemistry. 9: 874-881. PMID 28837163 DOI: 10.1038/Nchem.2754 |
0.351 |
|
2017 |
Rodgers JM, Abaskharon RM, Ding B, Chen J, Zhang W, Gai F. Fermi resonance as a means to determine the hydrogen-bonding status of two infrared probes. Physical Chemistry Chemical Physics : Pccp. PMID 28604875 DOI: 10.1039/C7Cp02442H |
0.611 |
|
2017 |
Hilaire MR, Ahmed IA, Lin CW, Jo H, DeGrado WF, Gai F. Blue fluorescent amino acid for biological spectroscopy and microscopy. Proceedings of the National Academy of Sciences of the United States of America. PMID 28533371 DOI: 10.1073/Pnas.1705586114 |
0.355 |
|
2017 |
Lin CW, Gai F. Microscopic nucleation and propagation rates of an alanine-based α-helix. Physical Chemistry Chemical Physics : Pccp. PMID 28165082 DOI: 10.1039/C6Cp08924K |
0.414 |
|
2017 |
Ding B, Mukherjee D, Chen J, Gai F. Do guanidinium and tetrapropylammonium ions specifically interact with aromatic amino acid side chains? Proceedings of the National Academy of Sciences of the United States of America. PMID 28096375 DOI: 10.1073/Pnas.1618071114 |
0.651 |
|
2016 |
Ahmed IA, Gai F. Simple Method to Introduce an Ester Infrared Probe into Proteins. Protein Science : a Publication of the Protein Society. PMID 27813296 DOI: 10.1002/Pro.3076 |
0.43 |
|
2016 |
Markiewicz BN, Lemmin T, Zhang W, Ahmed IA, Jo H, Fiorin G, Troxler T, DeGrado WF, Gai F. Infrared and fluorescence assessment of the hydration status of the tryptophan gate in the influenza A M2 proton channel. Physical Chemistry Chemical Physics : Pccp. PMID 27725984 DOI: 10.1039/C6Cp03426H |
0.336 |
|
2016 |
Mukherjee D, Gai F. Exciton CD Couplet Arising From Nitrile-Derivatized Aromatic Residues as a Structural Probe of Proteins. Analytical Biochemistry. PMID 27251434 DOI: 10.1016/J.Ab.2016.05.017 |
0.337 |
|
2016 |
Ding B, Hilaire MR, Gai F. Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function. The Journal of Physical Chemistry. B. PMID 27183318 DOI: 10.1021/Acs.Jpcb.6B03199 |
0.702 |
|
2016 |
Abaskharon RM, Gai F. Meandering Down the Energy Landscape of Protein Folding: Are We There Yet? Biophysical Journal. 110: 1924-32. PMID 27166801 DOI: 10.1016/J.Bpj.2016.03.030 |
0.363 |
|
2016 |
Abaskharon RM, Gai F. Direct measurement of the tryptophan-mediated photocleavage kinetics of a protein disulfide bond. Physical Chemistry Chemical Physics : Pccp. PMID 26997094 DOI: 10.1039/C6Cp00865H |
0.459 |
|
2016 |
Markiewicz BN, Mukherjee D, Troxler T, Gai F. On the Utility of 5-Cyanotryptophan Fluorescence as a Sensitive Probe of Protein Hydration. The Journal of Physical Chemistry. B. PMID 26783936 DOI: 10.1021/Acs.Jpcb.5B12233 |
0.446 |
|
2016 |
Gai F. Assessing and Manipulating Protein Folding Dynamics Biophysical Journal. 110: 196a. DOI: 10.1016/J.Bpj.2015.11.1093 |
0.451 |
|
2015 |
Oh KI, Fiorin G, Gai F. How Sensitive is the Amide I Vibration of the Polypeptide Backbone to Electric Fields? Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 26419214 DOI: 10.1002/Cphc.201500777 |
0.354 |
|
2015 |
Zhang W, Markiewicz BN, Doerksen RS, Smith Iii AB, Gai F. C[triple bond, length as m-dash]N stretching vibration of 5-cyanotryptophan as an infrared probe of protein local environment: what determines its frequency? Physical Chemistry Chemical Physics : Pccp. PMID 26343769 DOI: 10.1039/C5Cp04413H |
0.33 |
|
2015 |
Hilaire MR, Abaskharon RM, Gai F. Biomolecular Crowding Arising from Small Molecules, Molecular Constraints, Surface Packing, and Nano-Confinement. The Journal of Physical Chemistry Letters. 6: 2546-53. PMID 26266732 DOI: 10.1021/Acs.Jpclett.5B00957 |
0.356 |
|
2015 |
Abaskharon RM, Culik RM, Woolley GA, Gai F. Tuning the Attempt Frequency of Protein Folding Dynamics via Transition-State Rigidification: Application to Trp-cage. The Journal of Physical Chemistry Letters. 6: 521-526. PMID 26120378 DOI: 10.1021/Jz502654Q |
0.814 |
|
2015 |
Pazos IM, Ahmed IA, Berríos MI, Gai F. Sensing pH via p-cyanophenylalanine fluorescence: Application to determine peptide pKa and membrane penetration kinetics. Analytical Biochemistry. 483: 21-6. PMID 25935260 DOI: 10.1016/J.Ab.2015.04.026 |
0.333 |
|
2015 |
Oh KI, Smith-Dupont KB, Markiewicz BN, Gai F. Kinetics of Peptide Folding in Lipid Membranes. Biopolymers. PMID 25808575 DOI: 10.1002/Bip.22640 |
0.409 |
|
2015 |
Chuntonov L, Pazos IM, Ma J, Gai F. Kinetics of exchange between zero-, one-, and two-hydrogen-bonded states of methyl and ethyl acetate in methanol. The Journal of Physical Chemistry. B. 119: 4512-20. PMID 25738661 DOI: 10.1021/Acs.Jpcb.5B00745 |
0.729 |
|
2015 |
Mintzer MR, Troxler T, Gai F. p-Cyanophenylalanine and selenomethionine constitute a useful fluorophore-quencher pair for short distance measurements: application to polyproline peptides. Physical Chemistry Chemical Physics : Pccp. 17: 7881-7. PMID 25716887 DOI: 10.1039/C5Cp00050E |
0.402 |
|
2015 |
Ma J, Pazos IM, Zhang W, Culik RM, Gai F. Site-specific infrared probes of proteins. Annual Review of Physical Chemistry. 66: 357-77. PMID 25580624 DOI: 10.1146/Annurev-Physchem-040214-121802 |
0.781 |
|
2014 |
Markiewicz BN, Culik RM, Gai F. Tightening up the structure, lighting up the pathway: Application of molecular constraints and light to manipulate protein folding, self-assembly and function. Science China. Chemistry. 57: 1615-1624. PMID 25722715 DOI: 10.1007/S11426-014-5225-5 |
0.811 |
|
2014 |
Culik RM, Abaskharon RM, Pazos IM, Gai F. Experimental validation of the role of trifluoroethanol as a nanocrowder. The Journal of Physical Chemistry. B. 118: 11455-61. PMID 25215518 DOI: 10.1021/Jp508056W |
0.803 |
|
2014 |
Ghosh A, Wang J, Moroz YS, Korendovych IV, Zanni M, DeGrado WF, Gai F, Hochstrasser RM. 2D IR spectroscopy reveals the role of water in the binding of channel-blocking drugs to the influenza M2 channel. The Journal of Chemical Physics. 140: 235105. PMID 24952572 DOI: 10.1063/1.4881188 |
0.67 |
|
2014 |
Ma J, Pazos IM, Gai F. Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO). Proceedings of the National Academy of Sciences of the United States of America. 111: 8476-81. PMID 24912147 DOI: 10.1073/Pnas.1403224111 |
0.458 |
|
2014 |
Pazos IM, Ghosh A, Tucker MJ, Gai F. Ester carbonyl vibration as a sensitive probe of protein local electric field. Angewandte Chemie (International Ed. in English). 53: 6080-4. PMID 24788907 DOI: 10.1002/Anie.201402011 |
0.66 |
|
2014 |
Ghosh A, Tucker MJ, Gai F. 2D IR spectroscopy of histidine: probing side-chain structure and dynamics via backbone amide vibrations. The Journal of Physical Chemistry. B. 118: 7799-805. PMID 24712671 DOI: 10.1021/Jp411901M |
0.69 |
|
2014 |
Markiewicz BN, Yang L, Culik RM, Gao YQ, Gai F. How quickly can a β-hairpin fold from its transition state? The Journal of Physical Chemistry. B. 118: 3317-25. PMID 24611730 DOI: 10.1021/Jp500774Q |
0.803 |
|
2014 |
Markiewicz BN, Oyola R, Du D, Gai F. Aggregation gatekeeper and controlled assembly of Trpzip β-hairpins. Biochemistry. 53: 1146-54. PMID 24498924 DOI: 10.1021/Bi401568A |
0.389 |
|
2014 |
Montalvo GL, Gai F, Roder H, DeGrado WF. Slow folding-unfolding kinetics of an octameric β-peptide bundle. Acs Chemical Biology. 9: 276-81. PMID 24164344 DOI: 10.1021/Cb400621Y |
0.437 |
|
2013 |
Culik RM, Annavarapu S, Nanda V, Gai F. Using D-Amino Acids to Delineate the Mechanism of Protein Folding: Application to Trp-cage. Chemical Physics. 422. PMID 24307748 DOI: 10.1016/J.Chemphys.2013.01.021 |
0.797 |
|
2013 |
Zhu C, Dai Z, Liang H, Zhang T, Gai F, Lai L. Slow and bimolecular folding of a de novo designed monomeric protein DS119. Biophysical Journal. 105: 2141-8. PMID 24209859 DOI: 10.1016/J.Bpj.2013.09.014 |
0.436 |
|
2013 |
Markiewicz BN, Jo H, Culik RM, DeGrado WF, Gai F. Assessment of local friction in protein folding dynamics using a helix cross-linker. The Journal of Physical Chemistry. B. 117: 14688-96. PMID 24205975 DOI: 10.1021/Jp409334H |
0.806 |
|
2013 |
Measey TJ, Markiewicz BN, Gai F. Amide I Band and Photoinduced Disassembly of a Peptide Hydrogel. Chemical Physics Letters. 580: 135-140. PMID 23997272 DOI: 10.1016/J.Cplett.2013.06.055 |
0.341 |
|
2013 |
Pazos IM, Roesch RM, Gai F. Quenching of p-Cyanophenylalanine Fluorescence by Various Anions. Chemical Physics Letters. 563: 93-96. PMID 23645934 DOI: 10.1016/J.Cplett.2013.02.015 |
0.344 |
|
2013 |
Lin CW, Culik RM, Gai F. Using VIPT-jump to distinguish between different folding mechanisms: application to BBL and a Trpzip. Journal of the American Chemical Society. 135: 7668-73. PMID 23642153 DOI: 10.1021/Ja401473M |
0.807 |
|
2013 |
Guo L, Gai F. Simple method to enhance the photostability of the fluorescence reporter R6G for prolonged single-molecule studies. The Journal of Physical Chemistry. A. 117: 6164-70. PMID 23641719 DOI: 10.1021/Jp4003643 |
0.454 |
|
2012 |
Chow D, Guo L, Gai F, Goulian M. Fluorescence correlation spectroscopy measurements of the membrane protein TetA in Escherichia coli suggest rapid diffusion at short length scales. Plos One. 7: e48600. PMID 23119068 DOI: 10.1371/Journal.Pone.0048600 |
0.458 |
|
2012 |
Pazos IM, Gai F. Solute's perspective on how trimethylamine oxide, urea, and guanidine hydrochloride affect water's hydrogen bonding ability. The Journal of Physical Chemistry. B. 116: 12473-8. PMID 22998405 DOI: 10.1021/Jp307414S |
0.377 |
|
2012 |
Serrano AL, Bilsel O, Gai F. Native state conformational heterogeneity of HP35 revealed by time-resolved FRET. The Journal of Physical Chemistry. B. 116: 10631-8. PMID 22891809 DOI: 10.1021/Jp211296E |
0.697 |
|
2012 |
Measey TJ, Gai F. Light-triggered disassembly of amyloid fibrils. Langmuir : the Acs Journal of Surfaces and Colloids. 28: 12588-92. PMID 22867440 DOI: 10.1021/La302626D |
0.365 |
|
2012 |
Culik RM, Jo H, DeGrado WF, Gai F. Using thioamides to site-specifically interrogate the dynamics of hydrogen bond formation in β-sheet folding. Journal of the American Chemical Society. 134: 8026-9. PMID 22540162 DOI: 10.1021/Ja301681V |
0.795 |
|
2012 |
Wang YH, Collins A, Guo L, Smith-Dupont KB, Gai F, Svitkina T, Janmey PA. Divalent cation-induced cluster formation by polyphosphoinositides in model membranes. Journal of the American Chemical Society. 134: 3387-95. PMID 22280226 DOI: 10.1021/Ja208640T |
0.446 |
|
2012 |
Serrano AL, Waegele MM, Gai F. Spectroscopic studies of protein folding: linear and nonlinear methods. Protein Science : a Publication of the Protein Society. 21: 157-70. PMID 22109973 DOI: 10.1002/Pro.2006 |
0.817 |
|
2011 |
Waegele MM, Culik RM, Gai F. Site-Specific Spectroscopic Reporters of the Local Electric Field, Hydration, Structure, and Dynamics of Biomolecules. The Journal of Physical Chemistry Letters. 2: 2598-2609. PMID 22003429 DOI: 10.1021/Jz201161B |
0.8 |
|
2011 |
Culik RM, Serrano AL, Bunagan MR, Gai F. Achieving secondary structural resolution in kinetic measurements of protein folding: a case study of the folding mechanism of Trp-cage. Angewandte Chemie (International Ed. in English). 50: 10884-7. PMID 21956888 DOI: 10.1002/Anie.201104085 |
0.812 |
|
2011 |
Shandler SJ, Korendovych IV, Moore DT, Smith-Dupont KB, Streu CN, Litvinov RI, Billings PC, Gai F, Bennett JS, DeGrado WF. Computational design of a β-peptide that targets transmembrane helices. Journal of the American Chemical Society. 133: 12378-81. PMID 21780757 DOI: 10.1021/Ja204215F |
0.355 |
|
2011 |
Serrano AL, Tucker MJ, Gai F. Direct assessment of the α-helix nucleation time. The Journal of Physical Chemistry. B. 115: 7472-8. PMID 21568273 DOI: 10.1021/Jp200628B |
0.772 |
|
2011 |
Rogers JM, Polishchuk AL, Guo L, Wang J, DeGrado WF, Gai F. Photoinduced electron transfer and fluorophore motion as a probe of the conformational dynamics of membrane proteins: application to the influenza a M2 proton channel. Langmuir : the Acs Journal of Surfaces and Colloids. 27: 3815-21. PMID 21401044 DOI: 10.1021/La200480D |
0.669 |
|
2011 |
Waegele MM, Gai F. Power-law dependence of the melting temperature of ubiquitin on the volume fraction of macromolecular crowders. The Journal of Chemical Physics. 134: 095104. PMID 21385002 DOI: 10.1063/1.3556671 |
0.701 |
|
2011 |
Guo L, Smith-Dupont KB, Gai F. Diffusion as a probe of peptide-induced membrane domain formation. Biochemistry. 50: 2291-7. PMID 21332237 DOI: 10.1021/Bi102068J |
0.453 |
|
2011 |
Donald JE, Zhang Y, Fiorin G, Carnevale V, Slochower DR, Gai F, Klein ML, DeGrado WF. Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusion. Proceedings of the National Academy of Sciences of the United States of America. 108: 3958-63. PMID 21321234 DOI: 10.1073/Pnas.1019668108 |
0.376 |
|
2011 |
Fiorin G, Donald JE, Zhang Y, Carnevale V, Slochower DR, Gai F, Klein ML, DeGrado WF. Association of Transmembrane Helices in Viral Fusion Peptides Suggests a Protein-Centric Mechanism of Membrane Fusion Biophysical Journal. 100: 633a. DOI: 10.1016/J.Bpj.2010.12.3637 |
0.417 |
|
2011 |
Culik RM, Serrano AL, Bunagan MR, Gai F. Cover Picture: Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp-cage (Angew. Chem. Int. Ed. 46/2011) Angewandte Chemie International Edition. 50: 10735-10735. DOI: 10.1002/Anie.201106049 |
0.802 |
|
2011 |
Culik RM, Serrano AL, Bunagan MR, Gai F. Titelbild: Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp-cage (Angew. Chem. 46/2011) Angewandte Chemie. 123: 10923-10923. DOI: 10.1002/Ange.201106049 |
0.803 |
|
2010 |
Urbanek DC, Vorobyev DY, Serrano AL, Gai F, Hochstrasser RM. The Two Dimensional Vibrational Echo of a Nitrile Probe of the Villin HP35 Protein. The Journal of Physical Chemistry Letters. 1: 3311-3315. PMID 21132120 DOI: 10.1021/Jz101367D |
0.678 |
|
2010 |
Jo H, Culik RM, Korendovych IV, Degrado WF, Gai F. Selective incorporation of nitrile-based infrared probes into proteins via cysteine alkylation. Biochemistry. 49: 10354-6. PMID 21077670 DOI: 10.1021/Bi101711A |
0.805 |
|
2010 |
Waegele MM, Gai F. Infrared study of the folding mechanism of a helical hairpin: porcine PYY. Biochemistry. 49: 7659-64. PMID 20666415 DOI: 10.1021/Bi100851C |
0.782 |
|
2010 |
Guo L, Gai F. Heterogeneous diffusion of a membrane-bound pHLIP peptide. Biophysical Journal. 98: 2914-22. PMID 20550904 DOI: 10.1016/J.Bpj.2010.03.050 |
0.455 |
|
2010 |
Smith-Dupont KB, Guo L, Gai F. Diffusion as a probe of the heterogeneity of antimicrobial peptide-membrane interactions. Biochemistry. 49: 4672-8. PMID 20455545 DOI: 10.1021/Bi100426P |
0.457 |
|
2010 |
Waegele MM, Gai F. Computational Modeling of the Nitrile Stretching Vibration of 5-Cyanoindole in Water. The Journal of Physical Chemistry Letters. 1: 781-786. PMID 20436926 DOI: 10.1021/Jz900429Z |
0.725 |
|
2010 |
Serrano AL, Troxler T, Tucker MJ, Gai F. Photophysics of a Fluorescent Non-natural Amino Acid: p-Cyanophenylalanine. Chemical Physics Letters. 487: 303-306. PMID 20419080 DOI: 10.1016/J.Cplett.2010.01.058 |
0.726 |
|
2010 |
Montalvo G, Waegele MM, Shandler S, Gai F, DeGrado WF. Infrared signature and folding dynamics of a helical beta-peptide. Journal of the American Chemical Society. 132: 5616-8. PMID 20373737 DOI: 10.1021/Ja100459A |
0.767 |
|
2010 |
Rogers JM, Lippert LG, Gai F. Non-natural amino acid fluorophores for one- and two-step fluorescence resonance energy transfer applications. Analytical Biochemistry. 399: 182-9. PMID 20036210 DOI: 10.1016/J.Ab.2009.12.027 |
0.678 |
|
2010 |
GAI F, RICH RL, CHEN Y, PETRICH JW. ChemInform Abstract: Probing Solvation by Alcohols and Water with 7-Azaindole. Cheminform. 26: no-no. DOI: 10.1002/chin.199506299 |
0.625 |
|
2009 |
Waegele MM, Tucker MJ, Gai F. 5-Cyanotryptophan as an Infrared Probe of Local Hydration Status of Proteins. Chemical Physics Letters. 478: 249-253. PMID 20161057 DOI: 10.1016/J.Cplett.2009.07.058 |
0.795 |
|
2009 |
Levental I, Byfield FJ, Chowdhury P, Gai F, Baumgart T, Janmey PA. Cholesterol-dependent phase separation in cell-derived giant plasma-membrane vesicles. The Biochemical Journal. 424: 163-7. PMID 19811449 DOI: 10.1042/Bj20091283 |
0.678 |
|
2009 |
Mukherjee S, Waegele MM, Chowdhury P, Guo L, Gai F. Effect of macromolecular crowding on protein folding dynamics at the secondary structure level. Journal of Molecular Biology. 393: 227-36. PMID 19682997 DOI: 10.1016/J.Jmb.2009.08.016 |
0.83 |
|
2009 |
Bunagan MR, Gao J, Kelly JW, Gai F. Probing the folding transition state structure of the villin headpiece subdomain via side chain and backbone mutagenesis. Journal of the American Chemical Society. 131: 7470-6. PMID 19425552 DOI: 10.1021/Ja901860F |
0.798 |
|
2009 |
Tang J, Kang SG, Saven JG, Gai F. Characterization of the cofactor-induced folding mechanism of a zinc-binding peptide using computationally designed mutants. Journal of Molecular Biology. 389: 90-102. PMID 19361525 DOI: 10.1016/J.Jmb.2009.03.074 |
0.585 |
|
2009 |
Guo L, Park J, Lee T, Chowdhury P, Lim M, Gai F. Probing the role of hydration in the unfolding transitions of carbonmonoxy myoglobin and apomyoglobin. The Journal of Physical Chemistry. B. 113: 6158-63. PMID 19348439 DOI: 10.1021/Jp900009X |
0.782 |
|
2009 |
Tang J, Yin H, Qiu J, Tucker MJ, DeGrado WF, Gai F. Using two fluorescent probes to dissect the binding, insertion, and dimerization kinetics of a model membrane peptide. Journal of the American Chemical Society. 131: 3816-7. PMID 19256494 DOI: 10.1021/Ja809007F |
0.683 |
|
2009 |
Liu F, Dumont C, Zhu Y, DeGrado WF, Gai F, Gruebele M. A one-dimensional free energy surface does not account for two-probe folding kinetics of protein alpha(3)D. The Journal of Chemical Physics. 130: 061101. PMID 19222256 DOI: 10.1063/1.3077008 |
0.739 |
|
2009 |
Mukherjee S, Chowdhury P, Gai F. Effect of dehydration on the aggregation kinetics of two amyloid peptides. The Journal of Physical Chemistry. B. 113: 531-5. PMID 19132862 DOI: 10.1021/Jp809817S |
0.777 |
|
2008 |
Guo L, Chowdhury P, Glasscock JM, Gai F. Denaturant-induced expansion and compaction of a multi-domain protein: IgG. Journal of Molecular Biology. 384: 1029-36. PMID 19004457 DOI: 10.1016/J.Jmb.2008.03.006 |
0.765 |
|
2008 |
Glasscock JM, Zhu Y, Chowdhury P, Tang J, Gai F. Using an amino acid fluorescence resonance energy transfer pair to probe protein unfolding: application to the villin headpiece subdomain and the LysM domain. Biochemistry. 47: 11070-6. PMID 18816063 DOI: 10.1021/Bi8012406 |
0.834 |
|
2008 |
Tang J, Gai F. Dissecting the membrane binding and insertion kinetics of a pHLIP peptide. Biochemistry. 47: 8250-2. PMID 18636715 DOI: 10.1021/Bi801103X |
0.538 |
|
2008 |
Mukherjee S, Chowdhury P, Bunagan MR, Gai F. Folding kinetics of a naturally occurring helical peptide: implication of the folding speed limit of helical proteins. The Journal of Physical Chemistry. B. 112: 9146-50. PMID 18610960 DOI: 10.1021/Jp801721P |
0.822 |
|
2008 |
Xu Y, Bunagan MR, Tang J, Gai F. Probing the kinetic cooperativity of beta-sheet folding perpendicular to the strand direction. Biochemistry. 47: 2064-70. PMID 18197708 DOI: 10.1021/Bi702195C |
0.802 |
|
2007 |
Guo L, Chowdhury P, Fang J, Gai F. Heterogeneous and anomalous diffusion inside lipid tubules. The Journal of Physical Chemistry. B. 111: 14244-9. PMID 18052149 DOI: 10.1021/Jp076562N |
0.722 |
|
2007 |
Tang J, Signarvic RS, DeGrado WF, Gai F. Role of helix nucleation in the kinetics of binding of mastoparan X to phospholipid bilayers. Biochemistry. 46: 13856-63. PMID 17994771 DOI: 10.1021/Bi7018404 |
0.603 |
|
2007 |
Mukherjee S, Chowdhury P, DeGrado WF, Gai F. Site-specific hydration status of an amphipathic peptide in AOT reverse micelles. Langmuir : the Acs Journal of Surfaces and Colloids. 23: 11174-9. PMID 17910485 DOI: 10.1021/La701686G |
0.776 |
|
2007 |
Du D, Bunagan MR, Gai F. The effect of charge-charge interactions on the kinetics of alpha-helix formation. Biophysical Journal. 93: 4076-82. PMID 17704172 DOI: 10.1529/Biophysj.107.108548 |
0.796 |
|
2007 |
Wang T, Zhou Z, Bunagan MR, Du D, Bai Y, Gai F. Probing the folding intermediate of Rd-apocyt b562 by protein engineering and infrared T-jump. Protein Science : a Publication of the Protein Society. 16: 1176-83. PMID 17473017 DOI: 10.1110/Ps.062505607 |
0.799 |
|
2007 |
Chowdhury P, Wang W, Lavender S, Bunagan MR, Klemke JW, Tang J, Saven JG, Cooperman BS, Gai F. Fluorescence correlation spectroscopic study of serpin depolymerization by computationally designed peptides. Journal of Molecular Biology. 369: 462-73. PMID 17442346 DOI: 10.1016/J.Jmb.2007.03.042 |
0.796 |
|
2007 |
Mukherjee S, Chowdhury P, Gai F. Infrared study of the effect of hydration on the amide I band and aggregation properties of helical peptides. The Journal of Physical Chemistry. B. 111: 4596-602. PMID 17419612 DOI: 10.1021/Jp0689060 |
0.776 |
|
2007 |
Gai F, Du D, Xu Y. Infrared temperature-jump study of the folding dynamics of alpha-helices and beta-hairpins. Methods in Molecular Biology (Clifton, N.J.). 350: 1-20. PMID 16957314 DOI: 10.1385/1-59745-189-4:1 |
0.548 |
|
2006 |
Tang J, Gai F. A millisecond infrared stopped-flow apparatus. Applied Spectroscopy. 60: 1477-81. PMID 17217599 DOI: 10.1366/000370206779321328 |
0.52 |
|
2006 |
Xu Y, Purkayastha P, Gai F. Nanosecond folding dynamics of a three-stranded beta-sheet. Journal of the American Chemical Society. 128: 15836-42. PMID 17147395 DOI: 10.1021/Ja064865+ |
0.702 |
|
2006 |
Bunagan MR, Cristian L, DeGrado WF, Gai F. Truncation of a cross-linked GCN4-p1 coiled coil leads to ultrafast folding. Biochemistry. 45: 10981-6. PMID 16953584 DOI: 10.1021/Bi0606142 |
0.803 |
|
2006 |
Tucker MJ, Oyola R, Gai F. A novel fluorescent probe for protein binding and folding studies: p-cyano-phenylalanine. Biopolymers. 83: 571-6. PMID 16917881 DOI: 10.1002/Bip.20587 |
0.61 |
|
2006 |
Mukherjee S, Chowdhury P, Gai F. Tuning the cooperativity of the helix-coil transition by aqueous reverse micelles. The Journal of Physical Chemistry. B. 110: 11615-9. PMID 16800453 DOI: 10.1021/Jp062362K |
0.774 |
|
2006 |
Tucker MJ, Tang J, Gai F. Probing the kinetics of membrane-mediated helix folding. The Journal of Physical Chemistry. B. 110: 8105-9. PMID 16610913 DOI: 10.1021/Jp060900N |
0.695 |
|
2006 |
Park S, Xu Y, Stowell XF, Gai F, Saven JG, Boder ET. Limitations of yeast surface display in engineering proteins of high thermostability. Protein Engineering, Design & Selection : Peds. 19: 211-7. PMID 16537642 DOI: 10.1093/Protein/Gzl003 |
0.517 |
|
2006 |
Bunagan MR, Yang X, Saven JG, Gai F. Ultrafast folding of a computationally designed Trp-cage mutant: Trp2-cage. The Journal of Physical Chemistry. B. 110: 3759-63. PMID 16494434 DOI: 10.1021/Jp055288Z |
0.797 |
|
2006 |
Du D, Tucker MJ, Gai F. Understanding the mechanism of beta-hairpin folding via phi-value analysis. Biochemistry. 45: 2668-78. PMID 16489760 DOI: 10.1021/Bi052039S |
0.612 |
|
2006 |
Xu Y, Wang T, Gai F. Strange temperature dependence of the folding rate of a 16-residue β-hairpin Chemical Physics. 323: 21-27. DOI: 10.1016/J.Chemphys.2005.08.034 |
0.384 |
|
2005 |
Tucker MJ, Oyola R, Gai F. Conformational distribution of a 14-residue peptide in solution: a fluorescence resonance energy transfer study. The Journal of Physical Chemistry. B. 109: 4788-95. PMID 16851563 DOI: 10.1021/Jp044347Q |
0.613 |
|
2005 |
Wang T, Lau WL, DeGrado WF, Gai F. T-jump infrared study of the folding mechanism of coiled-coil GCN4-p1. Biophysical Journal. 89: 4180-7. PMID 16150962 DOI: 10.1529/Biophysj.105.068809 |
0.442 |
|
2005 |
Purkayastha P, Klemke JW, Lavender S, Oyola R, Cooperman BS, Gai F. Alpha 1-antitrypsin polymerization: a fluorescence correlation spectroscopic study. Biochemistry. 44: 2642-9. PMID 15709777 DOI: 10.1021/Bi048662E |
0.689 |
|
2004 |
Wang T, Zhu Y, Getahun Z, Du D, Huang CY, Degrado WF, Gai F. Length Dependent Helix-Coil Transition Kinetics of Nine Alanine-Based Peptides. The Journal of Physical Chemistry. B. 108. PMID 24307864 DOI: 10.1021/Jp037272J |
0.79 |
|
2004 |
Du D, Zhu Y, Huang CY, Gai F. Understanding the key factors that control the rate of beta-hairpin folding. Proceedings of the National Academy of Sciences of the United States of America. 101: 15915-20. PMID 15520391 DOI: 10.1073/Pnas.0405904101 |
0.775 |
|
2004 |
Wang T, Xu Y, Du D, Gai F. Determining beta-sheet stability by Fourier transform infrared difference spectra. Biopolymers. 75: 163-72. PMID 15356870 DOI: 10.1002/Bip.20101 |
0.485 |
|
2004 |
Tucker MJ, Getahun Z, Nanda V, DeGrado WF, Gai F. A new method for determining the local environment and orientation of individual side chains of membrane-binding peptides. Journal of the American Chemical Society. 126: 5078-9. PMID 15099085 DOI: 10.1021/Ja032015D |
0.584 |
|
2004 |
Snow CD, Qiu L, Du D, Gai F, Hagen SJ, Pande VS. Trp zipper folding kinetics by molecular dynamics and temperature-jump spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 101: 4077-82. PMID 15020773 DOI: 10.1073/Pnas.0305260101 |
0.429 |
|
2004 |
Wang T, Zhu Y, Gai F. Folding of A Three-Helix Bundle at the Folding Speed Limit Journal of Physical Chemistry B. 108: 3694-3697. DOI: 10.1021/Jp049652Q |
0.751 |
|
2004 |
Zhu Y, Fu X, Wang T, Tamura A, Takada S, Saven JG, Gai F. Guiding the search for a protein's maximum rate of folding Chemical Physics. 307: 99-109. DOI: 10.1016/J.Chemphys.2004.05.008 |
0.776 |
|
2003 |
Zhu Y, Alonso DO, Maki K, Huang CY, Lahr SJ, Daggett V, Roder H, DeGrado WF, Gai F. Ultrafast folding of alpha3D: a de novo designed three-helix bundle protein. Proceedings of the National Academy of Sciences of the United States of America. 100: 15486-91. PMID 14671331 DOI: 10.1073/Pnas.2136623100 |
0.813 |
|
2003 |
Xu Y, Oyola R, Gai F. Infrared study of the stability and folding kinetics of a 15-residue beta-hairpin. Journal of the American Chemical Society. 125: 15388-94. PMID 14664583 DOI: 10.1021/Ja037053B |
0.536 |
|
2003 |
Getahun Z, Huang CY, Wang T, De León B, DeGrado WF, Gai F. Using nitrile-derivatized amino acids as infrared probes of local environment. Journal of the American Chemical Society. 125: 405-11. PMID 12517152 DOI: 10.1021/Ja0285262 |
0.564 |
|
2003 |
Huang CY, Wang T, Gai F. Temperature dependence of the CN stretching vibration of a nitrile-derivatized phenylalanine in water Chemical Physics Letters. 371: 731-738. DOI: 10.1016/S0009-2614(03)00353-1 |
0.504 |
|
2003 |
Wang T, Du D, Gai F. Helix-coil kinetics of two 14-residue peptides Chemical Physics Letters. 370: 842-848. DOI: 10.1016/S0009-2614(03)00223-9 |
0.421 |
|
2002 |
Huang CY, He S, DeGrado WF, McCafferty DG, Gai F. Light-induced helix formation. Journal of the American Chemical Society. 124: 12674-5. PMID 12392410 DOI: 10.1021/Ja028084U |
0.57 |
|
2002 |
Huang CY, Getahun Z, Zhu Y, Klemke JW, DeGrado WF, Gai F. Helix formation via conformation diffusion search. Proceedings of the National Academy of Sciences of the United States of America. 99: 2788-93. PMID 11867741 DOI: 10.1073/Pnas.052700099 |
0.795 |
|
2001 |
Huang CY, Getahun Z, Wang T, DeGrado WF, Gai F. Time-resolved infrared study of the helix-coil transition using (13)C-labeled helical peptides. Journal of the American Chemical Society. 123: 12111-2. PMID 11724630 DOI: 10.1021/Ja016631Q |
0.556 |
|
2001 |
Huang CY, Klemke JW, Getahun Z, DeGrado WF, Gai F. Temperature-dependent helix-coil transition of an alanine based peptide. Journal of the American Chemical Society. 123: 9235-8. PMID 11562202 DOI: 10.1021/Ja0158814 |
0.572 |
|
2000 |
Leeson DT, Gai F, Rodriguez HM, Gregoret LM, Dyer RB. Protein folding and unfolding on a complex energy landscape. Proceedings of the National Academy of Sciences of the United States of America. 97: 2527-32. PMID 10681466 DOI: 10.1073/Pnas.040580397 |
0.6 |
|
1999 |
Andersen NH, Dyer RB, Fesinmeyer RM, Gai F, Liu Z, Neidigh JW, Tong H. Effect of hexafluoroisopropanol on the thermodynamics of peptide secondary structure formation [5] Journal of the American Chemical Society. 121: 9879-9880. DOI: 10.1021/Ja991829K |
0.526 |
|
1998 |
Gai F, Hasson KC, McDonald JC, Anfinrud PA. Chemical dynamics in proteins: the photoisomerization of retinal in bacteriorhodopsin. Science (New York, N.Y.). 279: 1886-91. PMID 9506931 DOI: 10.1126/Science.279.5358.1886 |
0.346 |
|
1998 |
Dyer RB, Gai F, Woodruff WH, Gilmanshin R, Callender RH. Infrared Studies of Fast Events in Protein Folding Accounts of Chemical Research. 31: 709-716. DOI: 10.1021/Ar970343A |
0.687 |
|
1997 |
Andel F, Hasson KC, Gai F, Anfinrud PA, Mathies RA. Femtosecond time-resolved spectroscopy of the primary photochemistry of phytochrome Biospectroscopy. 3: 421-433. DOI: 10.1002/(Sici)1520-6343(1997)3:6<421::Aid-Bspy1>3.0.Co;2-3 |
0.31 |
|
1996 |
Hasson KC, Gai F, Anfinrud PA. The photoisomerization of retinal in bacteriorhodospin: experimental evidence for a three-state model. Proceedings of the National Academy of Sciences of the United States of America. 93: 15124-9. PMID 8986774 DOI: 10.1073/Pnas.93.26.15124 |
0.326 |
|
1995 |
Rich RL, Gai F, Lane JW, Petrich JW, Schwabacher AW. Using 7-azatryptophan to probe small molecule-protein interactions on the picosecond time scale: The complex of avidin and biotinylated 7-azatryptophan Journal of the American Chemical Society. 117: 733-739. DOI: 10.1021/Ja00107A016 |
0.713 |
|
1994 |
Gai F, Rich RL, Petrich JW. Monophotonic Ionization of 7-Azaindole, Indole, and Their Derivatives and the Role of Overlapping Excited States. [Erratum to document cited in CA120:163221] Journal of the American Chemical Society. 116: 8859-8859. DOI: 10.1021/Ja00098A076 |
0.661 |
|
1994 |
Gai F, Rich RL, Petrich JW. Monophotonic ionization of 7-azaindole, indole, and their derivatives and the role of overlapping excited states Journal of the American Chemical Society. 116: 735-746. DOI: 10.1021/Ja00081A039 |
0.69 |
|
1994 |
Gai F, Fehr MJ, Petrich JW. Role of solvent in excited-state proton transfer in hypericin Journal of Physical Chemistry®. 98: 8352-8358. DOI: 10.1021/J100085A015 |
0.679 |
|
1994 |
Gai F, Fehr MJ, Petrich JW. Observation of excited-state tautomerization in the antiviral agent hypericin and identification of its fluorescent species Journal of Physical Chemistry. 98: 5784-5795. DOI: 10.1021/J100073A036 |
0.679 |
|
1994 |
Chen Y, Gai F, Petrich JW. Single-exponential fluorescence decay of the nonnatural amino acid 7-azatryptophan and the nonexponential fluorescence decay of tryptophan in water Journal of Physical Chemistry. 98: 2203-2209. DOI: 10.1021/J100059A039 |
0.702 |
|
1994 |
Chen Y, Gai F, Petrich JW. Solvation and excited-state proton transfer of 7-azaindole in alcohols Chemical Physics Letters. 222: 329-334. DOI: 10.1016/0009-2614(94)87069-1 |
0.694 |
|
1993 |
Chen Y, Gai F, Petrich JW. Solvation of 7-azaindole in alcohols and water: Evidence for concerted, excited-state, double-proton transfer in alcohols Journal of the American Chemical Society. 115: 10158-10166. DOI: 10.1021/Ja00075A035 |
0.681 |
|
1993 |
Gai F, Fehr MJ, Petrich JW. Ultrafast excited-state processes in the antiviral agent hypericin Journal of the American Chemical Society. 115: 3384-3385. DOI: 10.1021/Ja00061A069 |
0.666 |
|
1993 |
Négrerie M, Gai F, Lambry JC, Martin JL, Petrich JW. Photoionization and dynamic solvation of the excited states of 7-azaindole Journal of Physical Chemistry. 97: 5046-5049. DOI: 10.1021/J100121A032 |
0.682 |
|
1993 |
Rich RL, Chen Y, Neven D, Négrerie M, Gai F, Petrich JW. Steady-state and time-resolved fluorescence anisotropy of 7-azaindole and its derivatives Journal of Physical Chemistry. 97: 1781-1788. DOI: 10.1021/J100111A012 |
0.687 |
|
1993 |
Chen Y, Rich RL, Gai F, Petrich JW. Fluorescent species of 7-azaindole and 7-azatryptophan in water Journal of Physical Chemistry. 97: 1770-1780. DOI: 10.1021/J100111A011 |
0.675 |
|
1992 |
Gai F, Chen Y, Petrich JW. Nonradiative pathways of 7-azaindole in water Journal of the American Chemical Society. 114: 8343-8345. DOI: 10.1021/Ja00048A001 |
0.704 |
|
1991 |
Négrerie M, Gai F, Bellefeuille SM, Petrich JW. Photophysics of a novel optical probe: 7-Azaindole Journal of Physical Chemistry. 95: 8663-8670. DOI: 10.1021/J100175A046 |
0.647 |
|
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