Modeling protein folding: the beauty and power of simplicity.
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[1] 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.
[2] J. Onuchic,et al. Funnels, pathways, and the energy landscape of protein folding: A synthesis , 1994, Proteins.
[3] M. Hao,et al. STATISTICAL THERMODYNAMICS OF PROTEIN FOLDING : SEQUENCE DEPENDENCE , 1994 .
[4] T. Sosnick,et al. Molecular collapse: The rate‐limiting step in two‐state cytochrome c folding , 1996, Proteins.
[5] K. Dill,et al. Folding kinetics of proteins and copolymers , 1992 .
[6] P. Wolynes,et al. Optimal protein-folding codes from spin-glass theory. , 1992, Proceedings of the National Academy of Sciences of the United States of America.
[7] E. Shakhnovich,et al. Formation of unique structure in polypeptide chains. Theoretical investigation with the aid of a replica approach. , 1989, Biophysical chemistry.
[8] A Kolinski,et al. Dynamic Monte Carlo simulations of a new lattice model of globular protein folding, structure and dynamics. , 1991, Journal of molecular biology.
[9] Tobin R. Sosnick,et al. The role of helix formation in the folding of a fully α‐helical coiled coil , 1996 .
[10] E. Shakhnovich,et al. Statistical mechanics of proteins with "evolutionary selected" sequences. , 1994, Physical review. E, Statistical physics, plasmas, fluids, and related interdisciplinary topics.
[11] B Honig,et al. Free energy balance in protein folding. , 1995, Advances in protein chemistry.
[12] A. Fersht,et al. Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: a critical test of the protein engineering method of analysis. , 1993, Biochemistry.
[13] D. Thirumalai,et al. Folding kinetics of proteins : a model study , 1992 .
[14] Robert L. Baldwin,et al. Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A , 1995, Nature.
[15] R. L. Baldwin,et al. Kinetics of hydrogen bond breakage in the process of unfolding of ribonuclease A measured by pulsed hydrogen exchange. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[16] M. Karplus,et al. Proteins: A Theoretical Perspective of Dynamics, Structure, and Thermodynamics , 1988 .
[17] E. Shakhnovich,et al. Proteins with selected sequences fold into unique native conformation. , 1994, Physical review letters.
[18] H. Scheraga,et al. Conformational studies of poly‐L‐alanine in water , 1968, Biopolymers.
[19] R. Sauer,et al. Folded proteins occur frequently in libraries of random amino acid sequences. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[20] B Honig,et al. Adding backbone to protein folding: why proteins are polypeptides. , 1996, Folding & design.
[21] Karplus,et al. Protein folding bottlenecks: A lattice Monte Carlo simulation. , 1991, Physical review letters.
[22] R. Sauer,et al. P22 Arc repressor: transition state properties inferred from mutational effects on the rates of protein unfolding and refolding. , 1995, Biochemistry.
[23] E I Shakhnovich,et al. Is burst hydrophobic collapse necessary for protein folding? , 1995, Biochemistry.
[24] E I Shakhnovich,et al. Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first‐order phase transition , 1989, Biopolymers.
[25] T. Creighton,et al. Protein Folding , 1992 .
[26] M. Karplus,et al. How does a protein fold? , 1994, Nature.
[27] E. Shakhnovich,et al. Conserved residues and the mechanism of protein folding , 1996, Nature.
[28] R T Sauer,et al. Crystal structure, folding, and operator binding of the hyperstable Arc repressor mutant PL8. , 1995, Biochemistry.
[29] E I Shakhnovich,et al. Impact of local and non-local interactions on thermodynamics and kinetics of protein folding. , 1995, Journal of molecular biology.
[30] P. Privalov,et al. Energetics of protein structure. , 1995, Advances in protein chemistry.
[31] A. Chaffotte,et al. Kinetic resolution of peptide bond and side chain far-UV circular dichroism during the folding of hen egg white lysozyme. , 1992, Biochemistry.
[32] Tobin R. Sosnick,et al. The Role a-Helical of Helix Formation in the Folding of a Fully Coiled Coil , 1996 .
[33] E. Shakhnovich,et al. Engineering of stable and fast-folding sequences of model proteins. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[34] P. Privalov,et al. Thermodynamic puzzle of apomyoglobin unfolding. , 1994, Journal of molecular biology.
[35] Harold A. Scheraga,et al. MONTE CARLO SIMULATION OF A FIRST-ORDER TRANSITION FOR PROTEIN FOLDING , 1994 .
[36] Andreas Matouschek,et al. Transient folding intermediates characterized by protein engineering , 1990, Nature.
[37] E I Shakhnovich,et al. Specific nucleus as the transition state for protein folding: evidence from the lattice model. , 1994, Biochemistry.
[38] T. Ackermann. C. L. Brooks III, M. Karplus, B. M. Pettitt. Proteins: A Theoretical Perspective of Dynamics, Structure and Thermodynamics, Volume LXXI, in: Advances in Chemical Physics, John Wiley & Sons, New York 1988. 259 Seiten, Preis: US $ 65.25 , 1990 .
[39] Serrano,et al. Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2. , 1995, Folding & design.
[40] Douglas Poland,et al. Theory of helix-coil transitions in biopolymers , 1970 .