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Susan Marqusee - Publications

Affiliations: 
Biochemistry and Molecular Biology University of California, Berkeley, Berkeley, CA 
Area:
protein folding
Website:
http://zebra.berkeley.edu/

102 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
2018 Lim SA, Bolin ER, Marqusee S. Tracing a protein's folding pathway over evolutionary time using ancestral sequence reconstruction and hydrogen exchange. Elife. 7. PMID 30204082 DOI: 10.7554/eLife.38369  0.44
2017 Lim SA, Marqusee S. The burst-phase folding intermediate of ribonuclease H changes conformation over evolutionary history. Biopolymers. PMID 29152711 DOI: 10.1002/bip.23086  0.4
2016 Lim SA, Hart KM, Harms MJ, Marqusee S. Evolutionary trend toward kinetic stability in the folding trajectory of RNases H. Proceedings of the National Academy of Sciences of the United States of America. PMID 27799545 DOI: 10.1073/pnas.1611781113  0.44
2016 Wheeler LC, Lim SA, Marqusee S, Harms MJ. The thermostability and specificity of ancient proteins. Current Opinion in Structural Biology. 38: 37-43. PMID 27288744 DOI: 10.1016/j.sbi.2016.05.015  1
2016 Zhuravlev PI, Hinczewski M, Chakrabarti S, Marqusee S, Thirumalai D. Reply to Alberti: Are in vitro folding experiments relevant in vivo? Proceedings of the National Academy of Sciences of the United States of America. PMID 27226292 DOI: 10.1073/pnas.1603395113  1
2016 Zhuravlev PI, Hinczewski M, Chakrabarti S, Marqusee S, Thirumalai D. Force-dependent switch in protein unfolding pathways and transition-state movements. Proceedings of the National Academy of Sciences of the United States of America. PMID 26818842 DOI: 10.1073/pnas.1515730113  1
2015 Koulechova DA, Tripp KW, Horner G, Marqusee S. When the Scaffold Cannot Be Ignored: The Role of the Hydrophobic Core in Ligand Binding and Specificity. Journal of Molecular Biology. 427: 3316-26. PMID 26301601 DOI: 10.1016/j.jmb.2015.08.014  1
2015 Petzold C, Marceau AH, Miller KH, Marqusee S, Keck JL. Interaction with Single-stranded DNA-binding Protein Stimulates Escherichia coli Ribonuclease HI Enzymatic Activity. The Journal of Biological Chemistry. 290: 14626-36. PMID 25903123 DOI: 10.1074/jbc.M115.655134  1
2015 Guinn EJ, Jagannathan B, Marqusee S. Single-molecule chemo-mechanical unfolding reveals multiple transition state barriers in a small single-domain protein. Nature Communications. 6: 6861. PMID 25882479 DOI: 10.1038/ncomms7861  1
2015 Rosen LE, Marqusee S. Autonomously folding protein fragments reveal differences in the energy landscapes of homologous RNases H. Plos One. 10: e0119640. PMID 25803034 DOI: 10.1371/journal.pone.0119640  1
2015 Bowman GR, Bolin ER, Hart KM, Maguire BC, Marqusee S. Discovery of multiple hidden allosteric sites by combining Markov state models and experiments. Proceedings of the National Academy of Sciences of the United States of America. 112: 2734-9. PMID 25730859 DOI: 10.1073/pnas.1417811112  1
2015 Riedel C, Gabizon R, Wilson CA, Hamadani K, Tsekouras K, Marqusee S, Pressé S, Bustamante C. The heat released during catalytic turnover enhances the diffusion of an enzyme. Nature. 517: 227-30. PMID 25487146 DOI: 10.1038/nature14043  1
2015 Rosen LE, Kathuria SV, Matthews CR, Bilsel O, Marqusee S. Non-native structure appears in microseconds during the folding of E. coli RNase H. Journal of Molecular Biology. 427: 443-53. PMID 25311861 DOI: 10.1016/j.jmb.2014.10.003  1
2014 Hart KM, Harms MJ, Schmidt BH, Elya C, Thornton JW, Marqusee S. Thermodynamic system drift in protein evolution. Plos Biology. 12: e1001994. PMID 25386647 DOI: 10.1371/journal.pbio.1001994  1
2014 Rosen LE, Connell KB, Marqusee S. Evidence for close side-chain packing in an early protein folding intermediate previously assumed to be a molten globule. Proceedings of the National Academy of Sciences of the United States of America. 111: 14746-51. PMID 25258414 DOI: 10.1073/pnas.1410630111  1
2014 Pressé S, Peterson J, Lee J, Elms P, MacCallum JL, Marqusee S, Bustamante C, Dill K. Single molecule conformational memory extraction: p5ab RNA hairpin. The Journal of Physical Chemistry. B. 118: 6597-603. PMID 24898871 DOI: 10.1021/jp500611f  1
2014 Jha SK, Marqusee S. Kinetic evidence for a two-stage mechanism of protein denaturation by guanidinium chloride. Proceedings of the National Academy of Sciences of the United States of America. 111: 4856-61. PMID 24639503 DOI: 10.1073/pnas.1315453111  1
2013 Dimster-Denk D, Tripp KW, Marini NJ, Marqusee S, Rine J. Mono and dual cofactor dependence of human cystathionine β-synthase enzyme variants in vivo and in vitro. G3 (Bethesda, Md.). 3: 1619-28. PMID 23934999 DOI: 10.1534/g3.113.006916  1
2013 Jagannathan B, Marqusee S. Protein folding and unfolding under force. Biopolymers. 99: 860-9. PMID 23784721 DOI: 10.1002/bip.22321  1
2013 Hu W, Walters BT, Kan ZY, Mayne L, Rosen LE, Marqusee S, Englander SW. Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America. 110: 7684-9. PMID 23603271 DOI: 10.1073/pnas.1305887110  1
2013 Udgaonkar J, Marqusee S. Folding and binding. Current Opinion in Structural Biology. 23: 1-3. PMID 23374590 DOI: 10.1016/j.sbi.2013.01.002  1
2012 Elms PJ, Chodera JD, Bustamante CJ, Marqusee S. Limitations of constant-force-feedback experiments. Biophysical Journal. 103: 1490-9. PMID 23062341 DOI: 10.1016/j.bpj.2012.06.051  0.56
2012 Jagannathan B, Elms PJ, Bustamante C, Marqusee S. Direct observation of a force-induced switch in the anisotropic mechanical unfolding pathway of a protein. Proceedings of the National Academy of Sciences of the United States of America. 109: 17820-5. PMID 22949695 DOI: 10.1073/pnas.1201800109  1
2012 Elms PJ, Chodera JD, Bustamante C, Marqusee S. The molten globule state is unusually deformable under mechanical force. Proceedings of the National Academy of Sciences of the United States of America. 109: 3796-801. PMID 22355138 DOI: 10.1073/pnas.1115519109  1
2011 Miller KH, Marqusee S. Propensity for C-terminal domain swapping correlates with increased regional flexibility in the C-terminus of RNase A. Protein Science : a Publication of the Protein Society. 20: 1735-44. PMID 21805524 DOI: 10.1002/pro.708  1
2011 Cecconi C, Shank EA, Marqusee S, Bustamante C. DNA molecular handles for single-molecule protein-folding studies by optical tweezers. Methods in Molecular Biology (Clifton, N.J.). 749: 255-71. PMID 21674378 DOI: 10.1007/978-1-61779-142-0_18  1
2011 Bernstein R, Schmidt KL, Harbury PB, Marqusee S. Structural and kinetic mapping of side-chain exposure onto the protein energy landscape. Proceedings of the National Academy of Sciences of the United States of America. 108: 10532-7. PMID 21670244 DOI: 10.1073/pnas.1103629108  1
2010 Hanes MS, Ratcliff K, Marqusee S, Handel TM. Protein-protein binding affinities by pulse proteolysis: application to TEM-1/BLIP protein complexes. Protein Science : a Publication of the Protein Society. 19: 1996-2000. PMID 20669180 DOI: 10.1002/pro.467  1
2010 Shank EA, Cecconi C, Dill JW, Marqusee S, Bustamante C. The folding cooperativity of a protein is controlled by its chain topology. Nature. 465: 637-40. PMID 20495548 DOI: 10.1038/nature09021  1
2010 Ratcliff K, Marqusee S. Identification of residual structure in the unfolded state of ribonuclease H1 from the moderately thermophilic Chlorobium tepidum: comparison with thermophilic and mesophilic homologues. Biochemistry. 49: 5167-75. PMID 20491485 DOI: 10.1021/bi1001097  1
2010 Miller KH, Karr JR, Marqusee S. A hinge region cis-proline in ribonuclease A acts as a conformational gatekeeper for C-terminal domain swapping. Journal of Molecular Biology. 400: 567-78. PMID 20471398 DOI: 10.1016/j.jmb.2010.05.017  1
2009 Connell KB, Horner GA, Marqusee S. A single mutation at residue 25 populates the folding intermediate of E. coli RNase H and reveals a highly dynamic partially folded ensemble. Journal of Molecular Biology. 391: 461-70. PMID 19505477 DOI: 10.1016/j.jmb.2009.05.084  1
2009 Connell KB, Miller EJ, Marqusee S. The folding trajectory of RNase H is dominated by its topology and not local stability: a protein engineering study of variants that fold via two-state and three-state mechanisms. Journal of Molecular Biology. 391: 450-60. PMID 19501596 DOI: 10.1016/j.jmb.2009.05.085  1
2009 Ratcliff K, Corn J, Marqusee S. Structure, stability, and folding of ribonuclease H1 from the moderately thermophilic Chlorobium tepidum: comparison with thermophilic and mesophilic homologues. Biochemistry. 48: 5890-8. PMID 19408959 DOI: 10.1021/bi900305p  1
2009 Zhang CZ, Seog J, Dill J, Smith SB, Zhang FX, Cecconi C, Marqusee S, Bustamante C, Springer TA. What can we learn from mechanical unfolding of a single protein domain by optical tweezers Aiche Annual Meeting, Conference Proceedings 1
2008 Cecconi C, Shank EA, Dahlquist FW, Marqusee S, Bustamante C. Protein-DNA chimeras for single molecule mechanical folding studies with the optical tweezers. European Biophysics Journal : Ebj. 37: 729-38. PMID 18183383 DOI: 10.1007/s00249-007-0247-y  1
2007 Cellitti J, Llinas M, Echols N, Shank EA, Gillespie B, Kwon E, Crowder SM, Dahlquist FW, Alber T, Marqusee S. Exploring subdomain cooperativity in T4 lysozyme I: structural and energetic studies of a circular permutant and protein fragment. Protein Science : a Publication of the Protein Society. 16: 842-51. PMID 17400926 DOI: 10.1110/ps.062628607  1
2007 Cellitti J, Bernstein R, Marqusee S. Exploring subdomain cooperativity in T4 lysozyme II: uncovering the C-terminal subdomain as a hidden intermediate in the kinetic folding pathway. Protein Science : a Publication of the Protein Society. 16: 852-62. PMID 17400925 DOI: 10.1110/ps.062632807  1
2007 Park C, Zhou S, Gilmore J, Marqusee S. Energetics-based protein profiling on a proteomic scale: identification of proteins resistant to proteolysis. Journal of Molecular Biology. 368: 1426-37. PMID 17400245 DOI: 10.1016/j.jmb.2007.02.091  1
2007 Young TA, Skordalakes E, Marqusee S. Comparison of proteolytic susceptibility in phosphoglycerate kinases from yeast and E. coli: modulation of conformational ensembles without altering structure or stability. Journal of Molecular Biology. 368: 1438-47. PMID 17397866 DOI: 10.1016/j.jmb.2007.02.077  1
2007 Cecconi C, Shank EA, Marqusee S, Bustamante CJ. Studying protein folding with laser tweezers Proceedings of the International School of Physics "Enrico Fermi". 165: 145-160.  1
2006 Park C, Marqusee S. Quantitative determination of protein stability and ligand binding by pulse proteolysis. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit 20.11. PMID 18429306 DOI: 10.1002/0471140864.ps2011s46  1
2006 Freedman TS, Sondermann H, Friedland GD, Kortemme T, Bar-Sagi D, Marqusee S, Kuriyan J. A Ras-induced conformational switch in the Ras activator Son of sevenless. Proceedings of the National Academy of Sciences of the United States of America. 103: 16692-7. PMID 17075039 DOI: 10.1073/pnas.0608127103  1
2006 Wildes D, Anderson LM, Sabogal A, Marqusee S. Native state energetics of the Src SH2 domain: evidence for a partially structured state in the denatured ensemble. Protein Science : a Publication of the Protein Society. 15: 1769-79. PMID 16751610 DOI: 10.1110/ps.062136006  1
2006 de los Rios MA, Muralidhara BK, Wildes D, Sosnick TR, Marqusee S, Wittung-Stafshede P, Plaxco KW, Ruczinski I. On the precision of experimentally determined protein folding rates and phi-values. Protein Science : a Publication of the Protein Society. 15: 553-63. PMID 16501226 DOI: 10.1110/ps.051870506  1
2005 Cecconi C, Shank EA, Bustamante C, Marqusee S. Direct observation of the three-state folding of a single protein molecule. Science (New York, N.Y.). 309: 2057-60. PMID 16179479 DOI: 10.1126/science.1116702  1
2005 Park C, Marqusee S. Pulse proteolysis: a simple method for quantitative determination of protein stability and ligand binding. Nature Methods. 2: 207-12. PMID 15782190 DOI: 10.1038/nmeth740  1
2005 Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallée-Bélisle A, Main ER, Bemporad F, Qiu L, Teilum K, ... ... Marqusee S, et al. Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Science : a Publication of the Protein Society. 14: 602-16. PMID 15689503 DOI: 10.1110/ps.041205405  1
2005 Wildes D, Marqusee S. Hydrogen exchange and ligand binding: ligand-dependent and ligand-independent protection in the Src SH3 domain. Protein Science : a Publication of the Protein Society. 14: 81-8. PMID 15576569 DOI: 10.1110/ps.04990205  1
2004 Park C, Marqusee S. Probing the high energy states in proteins by proteolysis. Journal of Molecular Biology. 343: 1467-76. PMID 15491624 DOI: 10.1016/j.jmb.2004.08.085  1
2004 Park C, Marqusee S. Analysis of the stability of multimeric proteins by effective DeltaG and effective m-values. Protein Science : a Publication of the Protein Society. 13: 2553-8. PMID 15322294 DOI: 10.1110/ps.04811004  1
2004 Wildes D, Marqusee S. Hydrogen-exchange strategies applied to energetics of intermediate processes in protein folding. Methods in Enzymology. 380: 328-49. PMID 15051344 DOI: 10.1016/S0076-6879(04)80015-6  1
2004 Spudich GM, Miller EJ, Marqusee S. Destabilization of the Escherichia coli RNase H kinetic intermediate: switching between a two-state and three-state folding mechanism. Journal of Molecular Biology. 335: 609-18. PMID 14672667 DOI: 10.1016/j.jmb.2003.10.052  1
2003 Robic S, Guzman-Casado M, Sanchez-Ruiz JM, Marqusee S. Role of residual structure in the unfolded state of a thermophilic protein. Proceedings of the National Academy of Sciences of the United States of America. 100: 11345-9. PMID 14504401 DOI: 10.1073/pnas.1635051100  1
2003 Kim R, Lai L, Lee HH, Cheong GW, Kim KK, Wu Z, Yokota H, Marqusee S, Kim SH. On the mechanism of chaperone activity of the small heat-shock protein of Methanococcus jannaschii. Proceedings of the National Academy of Sciences of the United States of America. 100: 8151-5. PMID 12817080 DOI: 10.1073/pnas.1032940100  1
2003 Guzman-Casado M, Parody-Morreale A, Robic S, Marqusee S, Sanchez-Ruiz JM. Energetic evidence for formation of a pH-dependent hydrophobic cluster in the denatured state of Thermus thermophilus ribonuclease H. Journal of Molecular Biology. 329: 731-43. PMID 12787674 DOI: 10.1016/S0022-2836(03)00513-8  1
2002 Miller EJ, Fischer KF, Marqusee S. Experimental evaluation of topological parameters determining protein-folding rates. Proceedings of the National Academy of Sciences of the United States of America. 99: 10359-63. PMID 12149462 DOI: 10.1073/pnas.162219099  1
2002 Kern G, Pelton J, Marqusee S, Kern D. Structural properties of the histidine-containing loop in HIV-1 RNase H. Biophysical Chemistry. 96: 285-91. PMID 12034447 DOI: 10.1016/S0301-4622(02)00019-4  1
2002 Nicholson EM, Mo H, Prusiner SB, Cohen FE, Marqusee S. Differences between the prion protein and its homolog Doppel: a partially structured state with implications for scrapie formation. Journal of Molecular Biology. 316: 807-15. PMID 11866533 DOI: 10.1006/jmbi.2001.5347  1
2002 Hollien J, Marqusee S. Comparison of the folding processes of T. thermophilus and E. coli ribonucleases H. Journal of Molecular Biology. 316: 327-40. PMID 11851342 DOI: 10.1006/jmbi.2001.5346  1
2002 Spudich G, Lorenz S, Marqusee S. Propagation of a single destabilizing mutation throughout the Escherichia coli ribonuclease HI native state. Protein Science : a Publication of the Protein Society. 11: 522-8. PMID 11847275 DOI: 10.1110/ps.37202  1
2002 Robic S, Berger JM, Marqusee S. Contributions of folding cores to the thermostabilities of two ribonucleases H. Protein Science : a Publication of the Protein Society. 11: 381-9. PMID 11790848 DOI: 10.1110/ps.38602  1
2001 Goedken ER, Marqusee S. Native-state energetics of a thermostabilized variant of ribonuclease HI. Journal of Molecular Biology. 314: 863-71. PMID 11734003 DOI: 10.1006/jmbi.2001.5184  1
2001 Parker MJ, Marqusee S. A kinetic folding intermediate probed by native state hydrogen exchange. Journal of Molecular Biology. 305: 593-602. PMID 11152615 DOI: 10.1006/jmbi.2000.4314  1
2001 Goedken ER, Marqusee S. Co-crystal of Escherichia coli RNase HI with Mn2+ ions reveals two divalent metals bound in the active site. The Journal of Biological Chemistry. 276: 7266-71. PMID 11083878 DOI: 10.1074/jbc.M009626200  1
2000 Goedken ER, Keck JL, Berger JM, Marqusee S. Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease HI. Protein Science : a Publication of the Protein Society. 9: 1914-21. PMID 11106164 DOI: 10.1110/ps.9.10.1914  1
2000 Spudich G, Marqusee S. A change in the apparent m value reveals a populated intermediate under equilibrium conditions in Escherichia coli ribonuclease HI. Biochemistry. 39: 11677-83. PMID 10995235 DOI: 10.1021/bi000466u  1
2000 Fischer KF, Marqusee S. A rapid test for identification of autonomous folding units in proteins. Journal of Molecular Biology. 302: 701-12. PMID 10986128 DOI: 10.1006/jmbi.2000.4049  1
2000 Toth EA, Worby C, Dixon JE, Goedken ER, Marqusee S, Yeates TO. The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds. Journal of Molecular Biology. 301: 433-50. PMID 10926519 DOI: 10.1006/jmbi.2000.3970  1
2000 Parker MJ, Marqusee S. A statistical appraisal of native state hydrogen exchange data: evidence for a burst phase continuum? Journal of Molecular Biology. 300: 1361-75. PMID 10903874 DOI: 10.1006/jmbi.2000.3922  1
2000 Chamberlain AK, Marqusee S. Comparison of equilibrium and kinetic approaches for determining protein folding mechanisms. Advances in Protein Chemistry. 53: 283-328. PMID 10751947 DOI: 10.1016/S0065-3233(00)53006-X  1
1999 Chamberlain AK, Fischer KF, Reardon D, Handel TM, Marqusee AS. Folding of an isolated ribonuclease H core fragment. Protein Science : a Publication of the Protein Society. 8: 2251-7. PMID 10595528 DOI: 10.1110/ps.8.11.2251  1
1999 Goedken ER, Marqusee S. Metal binding and activation of the ribonuclease H domain from moloney murine leukemia virus. Protein Engineering. 12: 975-80. PMID 10585503  1
1999 Hollien J, Marqusee S. Structural distribution of stability in a thermophilic enzyme. Proceedings of the National Academy of Sciences of the United States of America. 96: 13674-8. PMID 10570131 DOI: 10.1073/pnas.96.24.13674  1
1999 Parker MJ, Marqusee S. The cooperativity of burst phase reactions explored. Journal of Molecular Biology. 293: 1195-210. PMID 10547295 DOI: 10.1006/jmbi.1999.3204  1
1999 Llinás M, Gillespie B, Dahlquist FW, Marqusee S. The energetics of T4 lysozyme reveal a hierarchy of conformations. Nature Structural Biology. 6: 1072-8. PMID 10542101 DOI: 10.1038/14956  1
1999 Raschke TM, Kho J, Marqusee S. Confirmation of the hierarchical folding of RNase H: a protein engineering study. Nature Structural Biology. 6: 825-31. PMID 10467093 DOI: 10.1038/12277  1
1999 Liu H, Farr-Jones S, Ulyanov NB, Llinas M, Marqusee S, Groth D, Cohen FE, Prusiner SB, James TL. Solution structure of Syrian hamster prion protein rPrP(90-231). Biochemistry. 38: 5362-77. PMID 10220323 DOI: 10.1021/bi982878x  1
1999 Hollien J, Marqusee S. A thermodynamic comparison of mesophilic and thermophilic ribonucleases H. Biochemistry. 38: 3831-6. PMID 10090773 DOI: 10.1021/bi982684h  1
1998 Keck JL, Goedken ER, Marqusee S. Activation/attenuation model for RNase H. A one-metal mechanism with second-metal inhibition. The Journal of Biological Chemistry. 273: 34128-33. PMID 9852071 DOI: 10.1074/jbc.273.51.34128  1
1998 Kern G, Handel T, Marqusee S. Characterization of a folding intermediate from HIV-1 ribonuclease H. Protein Science : a Publication of the Protein Society. 7: 2164-74. PMID 9792104 DOI: 10.1002/pro.5560071014  1
1998 Goedken ER, Marqusee S. Folding the ribonuclease H domain of Moloney murine leukemia virus reverse transcriptase requires metal binding or a short N-terminal extension. Proteins. 33: 135-43. PMID 9741851 DOI: 10.1002/(SICI)1097-0134(19981001)33:1<135::AID-PROT12>3.0.CO;2-M  1
1998 Llinás M, Marqusee S. Subdomain interactions as a determinant in the folding and stability of T4 lysozyme. Protein Science : a Publication of the Protein Society. 7: 96-104. PMID 9514264 DOI: 10.1002/pro.5560070110  1
1998 Raschke TM, Marqusee S. Hydrogen exchange studies of protein structure. Current Opinion in Biotechnology. 9: 80-6. PMID 9503592 DOI: 10.1016/S0958-1669(98)80088-8  1
1998 Chamberlain AK, Marqusee S. Molten globule unfolding monitored by hydrogen exchange in urea. Biochemistry. 37: 1736-42. PMID 9492739 DOI: 10.1021/bi972692i  1
1997 Chamberlain AK, Marqusee S. Touring the landscapes: partially folded proteins examined by hydrogen exchange. Structure (London, England : 1993). 5: 859-63. PMID 9261079  1
1997 Goedken ER, Raschke TM, Marqusee S. Importance of the C-terminal helix to the stability and enzymatic activity of Escherichia coli ribonuclease H. Biochemistry. 36: 7256-63. PMID 9188727 DOI: 10.1021/bi970060q  1
1997 Raschke TM, Marqusee S. The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nature Structural Biology. 4: 298-304. PMID 9095198 DOI: 10.1038/nsb0497-298  1
1997 Chamberlain AK, Handel TM, Marqusee S. Detection of protein unfolding and fluctuations by native state hydrogen exchange Techniques in Protein Chemistry. 8: 727-734. DOI: 10.1016/S1080-8914(97)80071-3  1
1997 Keck JL, Marqusee S. Metal activation and regulation of E. coli RNase H Techniques in Protein Chemistry. 8: 409-416. DOI: 10.1016/S1080-8914(97)80041-5  1
1996 Dabora JM, Pelton JG, Marqusee S. Structure of the acid state of Escherichia coli ribonuclease HI. Biochemistry. 35: 11951-8. PMID 8810899 DOI: 10.1021/bi9611671  1
1996 Chamberlain AK, Handel TM, Marqusee S. Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. Nature Structural Biology. 3: 782-7. PMID 8784352 DOI: 10.1038/nsb0996-782  1
1996 Keck JL, Marqusee S. The putative substrate recognition loop of Escherichia coli ribonuclease H is not essential for activity. The Journal of Biological Chemistry. 271: 19883-7. PMID 8702700 DOI: 10.1074/jbc.271.33.19883  1
1995 Keck JL, Marqusee S. Substitution of a highly basic helix/loop sequence into the RNase H domain of human immunodeficiency virus reverse transcriptase restores its Mn(2+)-dependent RNase H activity. Proceedings of the National Academy of Sciences of the United States of America. 92: 2740-4. PMID 7535929  1
1994 Dabora JM, Marqusee S. Equilibrium unfolding of Escherichia coli ribonuclease H: characterization of a partially folded state. Protein Science : a Publication of the Protein Society. 3: 1401-8. PMID 7833802 DOI: 10.1002/pro.5560030906  1
1994 Marqusee S, Sauer RT. Contributions of a hydrogen bond/salt bridge network to the stability of secondary and tertiary structure in lambda repressor. Protein Science : a Publication of the Protein Society. 3: 2217-25. PMID 7756981 DOI: 10.1002/pro.5560031207  1
1991 Marqusee S, Regan L. Deconstructing protein structure. Current Biology : Cb. 1: 207-8. PMID 15336120 DOI: 10.1016/0960-9822(91)90057-4  1
1991 Scholtz JM, Marqusee S, Baldwin RL, York EJ, Stewart JM, Santoro M, Bolen DW. Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water. Proceedings of the National Academy of Sciences of the United States of America. 88: 2854-8. PMID 2011594  1
1990 Padmanabhan S, Marqusee S, Ridgeway T, Laue TM, Baldwin RL. Relative helix-forming tendencies of nonpolar amino acids. Nature. 344: 268-70. PMID 2314462 DOI: 10.1038/344268a0  1
1989 Marqusee S, Robbins VH, Baldwin RL. Unusually stable helix formation in short alanine-based peptides. Proceedings of the National Academy of Sciences of the United States of America. 86: 5286-90. PMID 2748584  1
1987 Marqusee S, Baldwin RL. Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design. Proceedings of the National Academy of Sciences of the United States of America. 84: 8898-902. PMID 3122208  1
1985 Shoemaker KR, Kim PS, Brems DN, Marqusee S, York EJ, Chaiken IM, Stewart JM, Baldwin RL. Nature of the charged-group effect on the stability of the C-peptide helix. Proceedings of the National Academy of Sciences of the United States of America. 82: 2349-53. PMID 3857585 DOI: 10.1073/pnas.82.8.2349  1
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