Susan Marqusee

发表

Exploring subdomain cooperativity in T4 lysozyme II: Uncovering the C‐terminal subdomain as a hidden intermediate in the kinetic folding pathway

S. Marqusee, J. Cellitti, Jason Cellitti, 2007, Protein science : a publication of the Protein Society.

Energetic evidence for formation of a pH-dependent hydrophobic cluster in the denatured state of Thermus thermophilus ribonuclease H.

Srebrenka Robic, Antonio Parody-Morreale, S. Marqusee, 2003, Journal of molecular biology.

Comparison of proteolytic susceptibility in phosphoglycerate kinases from yeast and E. coli: modulation of conformational ensembles without altering structure or stability.

S. Marqusee, E. Skordalakes, Susan Marqusee, 2007, Journal of molecular biology.

A hinge region cis-proline in ribonuclease A acts as a conformational gatekeeper for C-terminal domain swapping.

S. Marqusee, Susan Marqusee, Katherine H Miller, 2010, Journal of molecular biology.

The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions

S. Marqusee, T. M. Raschke, Susan Marqusee, 1997, Nature Structural Biology.

Comparison of the folding processes of T. thermophilus and E. coli ribonucleases H.

S. Marqusee, J. Hollien, Susan Marqusee, 2002, Journal of molecular biology.

DNA molecular handles for single-molecule protein-folding studies by optical tweezers.

Carlos Bustamante, Elizabeth A Shank, C. Bustamante, 2011, Methods in molecular biology.

Kinetic evidence for a two-stage mechanism of protein denaturation by guanidinium chloride

Santosh Kumar Jha, S. Marqusee, S. Jha, 2014, Proceedings of the National Academy of Sciences.

Direct Observation of the Three-State Folding of a Single Protein Molecule

Carlos Bustamante, Elizabeth A Shank, C. Bustamante, 2005, Science.

Protein folding: Defining a “standard” set of experimental conditions and a preliminary kinetic data set of two‐state proteins

Kevin W Plaxco, Ingo Ruczinski, Fabrizio Chiti, 2005, Protein science : a publication of the Protein Society.

Characterization of a folding intermediate from HIV‐1 ribonuclease H

Gunther Kern, S. Marqusee, T. Handel, 1998, Protein science : a publication of the Protein Society.

Destabilization of the Escherichia coli RNase H kinetic intermediate: switching between a two-state and three-state folding mechanism.

S. Marqusee, G. Spudich, Erik J Miller, 2004, Journal of molecular biology.

Role of residual structure in the unfolded state of a thermophilic protein

Srebrenka Robic, S. Marqusee, J. M. Sanchez-Ruiz, 2003, Proceedings of the National Academy of Sciences of the United States of America.

The molten globule state is unusually deformable under mechanical force

John D Chodera, Carlos Bustamante, C. Bustamante, 2012, Proceedings of the National Academy of Sciences.

Analysis of the stability of multimeric proteins by effective ΔG and effective m‐values

Susan Marqusee, Chiwook Park, 2004, Protein science : a publication of the Protein Society.

Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH

Tracy M. Handel, S. Marqusee, T. Handel, 1996, Nature Structural Biology.

A robust approach to estimating rates from time-correlation functions

Vijay S. Pande, John D. Chodera, William C. Swope, 2011, 1108.2304.

Bayesian hidden Markov model analysis of single-molecule force spectroscopy: Characterizing kinetics under measurement uncertainty

John D. Chodera, Bettina Keller, Nina Singhal Hinrichs, 2011, 1108.1430.

Force-dependent switch in protein unfolding pathways and transition-state movements

Michael Hinczewski, D Thirumalai, Shaon Chakrabarti, 2015, Proceedings of the National Academy of Sciences.

Single Molecule Conformational Memory Extraction: P5ab RNA Hairpin

Justin L. MacCallum, Steve Pressé, Ken Dill, 2014, The journal of physical chemistry. B.

Interaction with Single-stranded DNA-binding Protein Stimulates Escherichia coli Ribonuclease HI Enzymatic Activity*

S. Marqusee, J. Keck, Susan Marqusee, 2015, The Journal of Biological Chemistry.

Folding of an isolated ribonuclease H core fragment

S. Marqusee, T. Handel, A. K. Chamberlain, 2008, Protein science : a publication of the Protein Society.

Protein-DNA chimeras for single molecule mechanical folding studies with the optical tweezers

Elizabeth A. Shank, Carlos Bustamante, Frederick W. Dahlquist, 2008, European Biophysics Journal.

Relative helix-forming tendencies of nonpolar amino acids

Robert L. Baldwin, Thomas M. Laue, R. L. Baldwin, 1990, Nature.

The heat released during catalytic turnover enhances the diffusion of an enzyme

Kambiz M. Hamadani, Steve Pressé, Carlos Bustamante, 2014, Nature.

Experimental evaluation of topological parameters determining protein-folding rates

S. Marqusee, Erik J Miller, Susan Marqusee, 2002, Proceedings of the National Academy of Sciences of the United States of America.

On the precision of experimentally determined protein folding rates and ϕ‐values

Kevin W Plaxco, Ingo Ruczinski, Tobin R Sosnick, 2006, Protein science : a publication of the Protein Society.

The energetics of T4 lysozyme reveal a hierarchy of conformations

Manuel Llinás, Frederick W. Dahlquist, F. Dahlquist, 1999, Nature Structural Biology.

The thermostability and specificity of ancient proteins.

Lucas C Wheeler, Michael J Harms, S. Marqusee, 2016, Current opinion in structural biology.

The folding cooperativity of a protein is controlled by its chain topology

Elizabeth A. Shank, Carlos Bustamante, C. Bustamante, 2010, Nature.