GB1 is not a two-state folder: identification and characterization of an on-pathway intermediate.

[1]  Rudesh D. Toofanny,et al.  A comprehensive multidimensional-embedded, one-dimensional reaction coordinate for protein unfolding/folding. , 2010, Biophysical journal.

[2]  W. Eaton,et al.  Distinguishing between protein dynamics and dye photophysics in single-molecule FRET experiments. , 2010, Biophysical journal.

[3]  Distinguishing between smooth and rough free energy barriers in protein folding. , 2009, Biochemistry.

[4]  William A Eaton,et al.  Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-by-photon trajectories , 2009, Proceedings of the National Academy of Sciences.

[5]  Alan R. Fersht,et al.  From the first protein structures to our current knowledge of protein folding: delights and scepticisms , 2008, Nature Reviews Molecular Cell Biology.

[6]  Peter G Wolynes,et al.  Variationally determined free energy profiles for structural models of proteins: characteristic temperatures for folding and trapping. , 2008, The journal of physical chemistry. B.

[7]  Andrzej Kolinski,et al.  Folding pathway of the b1 domain of protein G explored by multiscale modeling. , 2007, Biophysical journal.

[8]  John Orban,et al.  The design and characterization of two proteins with 88% sequence identity but different structure and function , 2007, Proceedings of the National Academy of Sciences.

[9]  M. Brunori,et al.  Identification and characterization of protein folding intermediates. , 2007, Biophysical chemistry.

[10]  M. Brunori,et al.  Kinetic folding mechanism of PDZ2 from PTP-BL. , 2005, Protein engineering, design & selection : PEDS.

[11]  Valerie Daggett,et al.  Simulation and experiment conspire to reveal cryptic intermediates and a slide from the nucleation-condensation to framework mechanism of folding. , 2005, Journal of molecular biology.

[12]  Martin Karplus,et al.  The role of sequence and structure in protein folding kinetics; the diffusion-collision model applied to proteins L and G. , 2004, Structure.

[13]  David A C Beck,et al.  Methods for molecular dynamics simulations of protein folding/unfolding in solution. , 2004, Methods.

[14]  Jun Shimada,et al.  Commitment and nucleation in the protein G transition state. , 2004, Journal of molecular biology.

[15]  A. Gronenborn,et al.  Insights into conformation and dynamics of protein GB1 during folding and unfolding by NMR. , 2004, Journal of molecular biology.

[16]  Valerie Daggett,et al.  Unifying features in protein-folding mechanisms , 2003, Proceedings of the National Academy of Sciences of the United States of America.

[17]  T. Kiefhaber,et al.  Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding. , 2003, Journal of molecular biology.

[18]  T. Sosnick,et al.  Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding. , 2002, Journal of molecular biology.

[19]  John Karanicolas,et al.  The origins of asymmetry in the folding transition states of protein L and protein G , 2002, Protein science : a publication of the Protein Society.

[20]  E. Shakhnovich,et al.  The ensemble folding kinetics of protein G from an all-atom Monte Carlo simulation , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[21]  T. Kiefhaber,et al.  Apparent two-state tendamistat folding is a sequential process along a defined route. , 2001, Journal of molecular biology.

[22]  D. Baker,et al.  Critical role of β-hairpin formation in protein G folding , 2000, Nature Structural Biology.

[23]  D Baker,et al.  Critical role of beta-hairpin formation in protein G folding. , 2000, Nature structural biology.

[24]  Soon-Ho Park,et al.  Folding dynamics of the B1 domain of protein G explored by ultrarapid mixing , 1999, Nature Structural Biology.

[25]  G. Marius Clore,et al.  Improving the Packing and Accuracy of NMR Structures with a Pseudopotential for the Radius of Gyration , 1999 .

[26]  Alternative Explanations for "Multistate" Kinetics in Protein Folding: Transient Aggregation and Changing Transition-State Ensembles , 1998 .

[27]  A. Fersht,et al.  The changing nature of the protein folding transition state: implications for the shape of the free-energy profile for folding. , 1998, Journal of molecular biology.

[28]  C. Brooks,et al.  A molecular dynamics simulation study of segment B1 of protein G , 1997, Proteins.

[29]  T. Kiefhaber,et al.  Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediate. , 1997, Journal of molecular biology.

[30]  Michael Levitt,et al.  Calibration and Testing of a Water Model for Simulation of the Molecular Dynamics of Proteins and Nucleic Acids in Solution , 1997 .

[31]  M. Oliveberg,et al.  Transient aggregates in protein folding are easily mistaken for folding intermediates. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[32]  H. Roder,et al.  Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease. , 1997, Biochemistry.

[33]  H. Roder,et al.  An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core. , 1997, Biochemistry.

[34]  J. M. Sauder,et al.  Kinetic mechanism of folding and unfolding of Rhodobacter capsulatus cytochrome c2. , 1996, Biochemistry.

[35]  A. Gronenborn,et al.  Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy , 1995, Protein science : a publication of the Protein Society.

[36]  A. Fersht,et al.  The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding. , 1995, Journal of molecular biology.

[37]  A. Fersht.  Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[38]  M. J. Parker,et al.  An integrated kinetic analysis of intermediates and transition states in protein folding reactions. , 1995, Journal of molecular biology.

[39]  M. Levitt,et al.  Potential energy function and parameters for simulations of the molecular dynamics of proteins and nucleic acids in solution , 1995 .

[40]  J. Onuchic,et al.  Funnels, pathways, and the energy landscape of protein folding: A synthesis , 1994, Proteins.

[41]  P. Alexander,et al.  Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G. , 1992, Biochemistry.

[42]  A. Fersht,et al.  Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. , 1991, Biochemistry.

[43]  D. W. Bolen,et al.  Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. , 1988, Biochemistry.

[44]  B. Lee,et al.  The interpretation of protein structures: estimation of static accessibility. , 1971, Journal of molecular biology.