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Recent Publications:
Protein-DNA chimeras for single molecule mechanical folding studies with the optical tweezers. Cecconi C, Shank EA, Dahlquist FW, Marqusee S, Bustamante C.(2008) Eur Biophys J. (epub ahead of print) (Link)
Energetics-based protein profiling on a proteomic scale: identification of proteins resistant to proteolysis. Park C, Zhou S, Gilmore J, Marqusee S. (2007) J Mol Biol. 368(5):1426-37. (Link)
Comparison of proteolytic susceptibility in phosphoglycerate kinases from yeast and E. coli: modulation of conformational ensembles without altering structure or stability. Young TA, Skordalakes E, Marqusee S. (2007) J Mol Biol. 368(5):1438-47. (Link)
Exploring subdomain cooperativity in T4 lysozyme I: structural and energetic studies of a circular permutant and protein fragment. Cellitti J, Llinas M, Echols N, Shank EA, Gillespie B, Kwon E, Crowder SM, Dahlquist FW, Alber T, Marqusee S.(2007) Protein Sci. 16(5):842-51. (Link)
Exploring subdomain cooperativity in T4 lysozyme II: uncovering the C-terminal subdomain as a hidden intermediate in the kinetic folding pathway. Cellitti J, Bernstein R, Marqusee S.(2007) Protein Sci. 16(5):852-62. (Link)
A Ras-induced conformational switch in the Ras activator Son of sevenless. Freedman TS, Sondermann H, Friedland GD, Kortemme T, Bar-Sagi D, Marqusee S, Kuriyan J.(2007) Proc Natl Acad Sci U S A. 103(45):16692-7. (Link)
Native state energetics of the Src SH2 domain: evidence for a partially structured state in the denatured ensemble. Wildes D, Anderson LM, Sabogal A, Marqusee S. (2006) Protein Science 15:1769-79. (Link)
On the precision of experimentally determined protein folding rates and phi-values. de los Rios MA, Muralidhara BK, Wildes D, Sosnick TR, Marqusee S, Wittung-Stafshede P, Plaxco KW, Ruczinski I. (2006) Protein Science 15:553-63. (Link)
Direct observation of the three-state folding of a single protein molecule. Cecconi C and Shank EA, Bustamante C, Marqusee S. (2005) Science 309: 2057-60. (Link)
Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding. Park C and Marqusee S. (2005) Nature Methods 2: 207-212. (Link)
Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai Y, Hagen SJ, Serrano L, Oliveberg M, Raleigh DP, Wittung-Stafshede P, Radford SE, Jackson SE, Sosnick TR, Marqusee S, Davidson AR, Plaxco KW. (2005) Protein Sci. 14:602-616. (Link)
Hydrogen exchange and ligand binding: ligand-dependent and ligand-independent protection in the Src SH3 domain. Wildes D and Marqusee S. (2005) Protein Sci. 14:81-88. (Link)
Probing the high-energy states in proteins by proteolysis. Park C and Marqusee S. (2004) J. Mol. Biol. 343, 1467-1476. (Link)
Analysis of the stability of multimeric proteins by effective delta G and effective m-values. Park C and Marqusee S. (2004) Protein Sci. 9:2553-2558. (Link)
Hydrogen-exchange strategies applied to protein ensembles. Wildes D and Marqusee S. (2004) Methods Enzymol. 380:328-49. (Link)
Destabilization of the Escherichia coli RNase H kinetic intermediate: switching between a two-state and three-state folding mechanism. Spudich GM, Miller EJ, Marqusee S. (2004) JMB 335(2):609-18. (Link)
Role of residual structure in the unfolded state of a thermophilic protein. Robic S, Guzman-Casado M, Sanchez-Ruiz JM, Marqusee S. (2003) PNAS 100(20):11345-9. (Link)
Energetic evidence for formation of a pH-dependent hydrophobic cluster in the denatured state of Thermus thermophilus ribonuclease H. Guzman-Casado M, Parody-Morreale A, Robic S, Marqusee S, Sanchez-Ruiz JM (2003) JMB 329(4):731-43.
Evaluating the role of contact order as a determinant of protein folding rates. Miller EJ, Fischer KF, and Marqusee S (2002) PNAS 16:10359-63.
Differences between PrP and its homolog Dpl: Implications for a partially structured state in the formation of PrPSc. Nicholson EJ, Mo H, Cohen FE, Prusiner SB, and Marqusee S (2002) JMB 316:807-15.
Propagation of a single destabilizing mutation throughout the E. coli ribonuclease HI native state. Spudich G, Lorenz S and Marqusee S (2002) Protein Science 11:522-8.
Comparison of the folding processes of T. thermophilus and E. coli ribonucleases H Hollien J and Marqusee S (2002) JMB 316:327-40.
Contributions of the folding cores to thermostability of two ribonucleases H. Robic S, Berger JM, and Marqusee S (2002) Protein Science, 11:381-9.
Native-state energetics of a thermostabilized variant of ribonuclease H. Goedken ER, and Marqusee S (2001) JMB 314:863-71.
A kinetic folding intermediate probed by native state exchange. Parker MJ and Marqusee S (2001) JMB 305: 593-602.
Co-crystal of E. coli RNase HI with Mn2+ reveals two divalent metals bound in the active site. Goedken ER and Marqusee S (2001) J. Biol. Chem. 276:7266-7271.
A rapid test for identification of autonomous folding units in proteins. Fischer KF and Marqusee S (2000) JMB 302, 701-712.
Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease HI.Goedken ER, Keck JL, Berger JM, Marqusee S. (2000) Protein Sci. 9:1914-21.
A change in the apparent m value reveals a populated intermediate under equilibrium conditions in Escherichia coli ribonuclease HI. Spudich G and Marqusee S. (2000) Biochemistry 39:11677-83.
The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds. Toth EA, Worby C, Dixon JE, Goedken ER, Marqusee S, Yeates TO. (2000) JMB 302:701-12.
A statistical appraisal of native state hydrogen exchange data: evidence for a burst phase continuum?Parker MJ and Marqusee S. (2000) JMB 301:433-50.
Comparison of equilibrium and kinetic approaches for determining protein folding mechanisms.Chamberlain AK and Marqusee S. (2000) Adv. Protein Chem. 53: 283-328.