Protein folding from a highly disordered denatured state: The folding pathway of chymotrypsin inhibitor 2 at atomic resolution
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Valerie Daggett | Alan R. Fersht | A. Fersht | S. Kazmirski | V. Daggett | S. Freund | Kam-Bo Wong | Stefan M. V. Freund | Steven L. Kazmirski | Kam-Bo Wong | Yee-Joo Tan | Y. Tan
[1] P. Kraulis. A program to produce both detailed and schematic plots of protein structures , 1991 .
[2] 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 .
[3] A. Fersht,et al. Structure of the transition state for folding of a protein derived from experiment and simulation. , 1996, Journal of molecular biology.
[4] M. Wittekind,et al. HNCACB, a High-Sensitivity 3D NMR Experiment to Correlate Amide-Proton and Nitrogen Resonances with the Alpha- and Beta-Carbon Resonances in Proteins , 1993 .
[5] F M Poulsen,et al. Refinement of the three-dimensional solution structure of barley serine proteinase inhibitor 2 and comparison with the structures in crystals. , 1991, Journal of molecular biology.
[6] A. Palmer,et al. Probing molecular motion by NMR. , 1997, Current opinion in structural biology.
[7] A. Fersht,et al. Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway. , 1995, Journal of molecular biology.
[8] B D Sykes,et al. Chemical shifts as a tool for structure determination. , 1994, Methods in enzymology.
[9] C. J. Bond,et al. Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding. , 2000, Journal of molecular biology.
[10] A. Fersht,et al. Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[11] W. Kabsch,et al. Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.
[12] R. Srinivasan,et al. The Flory isolated-pair hypothesis is not valid for polypeptide chains: implications for protein folding. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[13] A. Fersht,et al. Search for nucleation sites in smaller fragments of chymotrypsin inhibitor 2. , 1995, Journal of molecular biology.
[14] M Karplus,et al. "New view" of protein folding reconciled with the old through multiple unfolding simulations. , 1997, Science.
[15] M. Levitt,et al. Potential energy function and parameters for simulations of the molecular dynamics of proteins and nucleic acids in solution , 1995 .
[16] A. Fersht,et al. Synergy between simulation and experiment in describing the energy landscape of protein folding. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[17] A. Li,et al. Identification and characterization of the unfolding transition state of chymotrypsin inhibitor 2 by molecular dynamics simulations. , 1996, Journal of molecular biology.
[18] Jeffrey W. Peng,et al. Mapping of Spectral Density Functions Using Heteronuclear NMR Relaxation Measurements , 1992 .
[19] M. Karplus. Contact Electron‐Spin Coupling of Nuclear Magnetic Moments , 1959 .
[20] A. Li,et al. Investigation of the solution structure of chymotrypsin inhibitor 2 using molecular dynamics: comparison to x-ray crystallographic and NMR data. , 1995, Protein engineering.
[21] A. Fersht,et al. Following co-operative formation of secondary and tertiary structure in a single protein module. , 1997, Journal of molecular biology.
[22] Gerhard Wagner,et al. NMR relaxation and protein mobility , 1993 .
[23] A. Fersht,et al. Perturbed pKA-values in the denatured states of proteins. , 1995, Journal of molecular biology.
[24] Andrew B. Martin,et al. Single-molecule protein folding: diffusion fluorescence resonance energy transfer studies of the denaturation of chymotrypsin inhibitor 2. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[25] A. Fersht,et al. The structure of the transition state for the association of two fragments of the barley chymotrypsin inhibitor 2 to generate native-like protein: implications for mechanisms of protein folding. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[26] L. Kay,et al. Gradient-Enhanced Triple-Resonance Three-Dimensional NMR Experiments with Improved Sensitivity , 1994 .
[27] E A Merritt,et al. Raster3D Version 2.0. A program for photorealistic molecular graphics. , 1994, Acta crystallographica. Section D, Biological crystallography.
[28] A. Li,et al. Characterization of the transition state of protein unfolding by use of molecular dynamics: chymotrypsin inhibitor 2. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[29] I. Kuntz,et al. A molecular dynamics simulation of polyalanine: An analysis of equilibrium motions and helix–coil transitions , 1991, Biopolymers.
[30] A. Fersht,et al. Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[31] A. Fersht,et al. Mapping the transition state and pathway of protein folding by protein engineering , 1989, Nature.
[32] A. Fersht,et al. Direct observation of better hydration at the N terminus of an alpha-helix with glycine rather than alanine as the N-cap residue. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[33] Conrad C. Huang,et al. The MIDAS display system , 1988 .