TOUCHSTONE II: a new approach to ab initio protein structure prediction.
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[1] J. Skolnick,et al. TOUCHSTONEX: Protein structure prediction with sparse NMR data , 2003, Proteins.
[2] J. Skolnick. Monte Carlo Simulations of Protein Folding , 2003 .
[3] J. Skolnick,et al. Local energy landscape flattening: Parallel hyperbolic Monte Carlo sampling of protein folding , 2002, Proteins.
[4] J. Skolnick,et al. TOUCHSTONE: An ab initio protein structure prediction method that uses threading-based tertiary restraints , 2001, Proceedings of the National Academy of Sciences of the United States of America.
[5] P Rotkiewicz,et al. Generalized comparative modeling (GENECOMP): A combination of sequence comparison, threading, and lattice modeling for protein structure prediction and refinement , 2001, Proteins.
[6] Z. Ou-Yang,et al. Stretching single-stranded DNA: interplay of electrostatic, base-pairing, and base-pair stacking interactions. , 2001, Biophysical journal.
[7] D. Baker,et al. Prospects for ab initio protein structural genomics. , 2001, Journal of molecular biology.
[8] Adam Liwo,et al. Recent improvements in prediction of protein structure by global optimization of a potential energy function , 2001, Proceedings of the National Academy of Sciences of the United States of America.
[9] J Skolnick,et al. Defrosting the frozen approximation: PROSPECTOR— A new approach to threading , 2001, Proteins.
[10] Jeffrey Skolnick,et al. Finding the needle in a haystack: educing native folds from ambiguous ab initio protein structure predictions , 2001, J. Comput. Chem..
[11] C. Brooks,et al. From folding theories to folding proteins: a review and assessment of simulation studies of protein folding and unfolding. , 2001, Annual review of physical chemistry.
[12] R. Elber,et al. Distance‐dependent, pair potential for protein folding: Results from linear optimization , 2000, Proteins.
[13] D. Baker,et al. A surprising simplicity to protein folding , 2000, Nature.
[14] A. Panchenko,et al. Combination of threading potentials and sequence profiles improves fold recognition. , 2000, Journal of molecular biology.
[15] M Vendruscolo,et al. Can a pairwise contact potential stabilize native protein folds against decoys obtained by threading? , 2000, Proteins.
[16] T. N. Bhat,et al. The Protein Data Bank , 2000, Nucleic Acids Res..
[17] D T Jones,et al. Protein secondary structure prediction based on position-specific scoring matrices. , 1999, Journal of molecular biology.
[18] Gerard T. Barkema,et al. Monte Carlo Methods in Statistical Physics , 1999 .
[19] D. Baker,et al. Improved recognition of native‐like protein structures using a combination of sequence‐dependent and sequence‐independent features of proteins , 1999, Proteins.
[20] D. Baker,et al. Clustering of low-energy conformations near the native structures of small proteins. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[21] J. Skolnick,et al. Assembly of protein structure from sparse experimental data: An efficient Monte Carlo model , 1998, Proteins.
[22] J. Skolnick,et al. An Efficient Monte Carlo Model of Protein Chains. Modeling the Short-Range Correlations between Side Group Centers of Mass , 1998 .
[23] Richard Hughey,et al. Hidden Markov models for detecting remote protein homologies , 1998, Bioinform..
[24] David C. Jones,et al. Progress in protein structure prediction. , 1997, Current opinion in structural biology.
[25] A. Godzik,et al. Derivation and testing of pair potentials for protein folding. When is the quasichemical approximation correct? , 1997, Protein science : a publication of the Protein Society.
[26] N. Guex,et al. SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modeling , 1997, Electrophoresis.
[27] R Sánchez,et al. Evaluation of comparative protein structure modeling by MODELLER‐3 , 1997, Proteins.
[28] B. Rost,et al. Combining evolutionary information and neural networks to predict protein secondary structure , 1994, Proteins.
[29] J. Skolnick,et al. Monte carlo simulations of protein folding. I. Lattice model and interaction scheme , 1994, Proteins.
[30] F. James. MINUIT Function Minimization and Error Analysis: Reference Manual Version 94.1 , 1994 .
[31] S. Benner,et al. Patterns of divergence in homologous proteins as indicators of secondary and tertiary structure: a prediction of the structure of the catalytic domain of protein kinases. , 1991, Advances in enzyme regulation.
[32] D. Eisenberg,et al. A method to identify protein sequences that fold into a known three-dimensional structure. , 1991, Science.
[33] W. Kabsch,et al. Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.
[34] R. Doolittle,et al. A simple method for displaying the hydropathic character of a protein. , 1982, Journal of molecular biology.
[35] K. R. Woods,et al. Prediction of protein antigenic determinants from amino acid sequences. , 1981, Proceedings of the National Academy of Sciences of the United States of America.
[36] C. Anfinsen. Principles that govern the folding of protein chains. , 1973, Science.
[37] S. Lowen. The Biophysical Journal , 1960, Nature.