New Programs for Protein Tertiary Structure Prediction
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[1] N. Go,et al. Ring Closure and Local Conformational Deformations of Chain Molecules , 1970 .
[2] F M Richards,et al. Areas, volumes, packing and protein structure. , 1977, Annual review of biophysics and bioengineering.
[3] G J Williams,et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1978, Archives of biochemistry and biophysics.
[4] M. Karplus,et al. An analysis of incorrectly folded protein models. Implications for structure predictions. , 1984, Journal of molecular biology.
[5] G. Rose,et al. Loops in globular proteins: a novel category of secondary structure. , 1986, Science.
[6] T. A. Jones,et al. Using known substructures in protein model building and crystallography. , 1986, The EMBO journal.
[7] J. Moult,et al. An algorithm for determining the conformation of polypeptide segments in proteins by systematic search , 1986, Proteins.
[8] A. Lesk,et al. The relation between the divergence of sequence and structure in proteins. , 1986, The EMBO journal.
[9] A. D. McLachlan,et al. Solvation energy in protein folding and binding , 1986, Nature.
[10] C. Levinthal,et al. Predicting antibody hypervariable loop conformations II: Minimization and molecular dynamics studies of MCPC603 from many randomly generated loop conformations , 1986, Proteins.
[11] Y. Satow,et al. Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A. , 1985, Journal of molecular biology.
[12] N. Patel,et al. Characterization and cloning of fasciclin III: A glycoprotein expressed on a subset of neurons and axon pathways in Drosophila , 1987, Cell.
[13] T. L. Blundell,et al. Knowledge-based prediction of protein structures and the design of novel molecules , 1987, Nature.
[14] C. Levinthal,et al. Predicting antibody hypervariable loop conformation. I. Ensembles of random conformations for ringlike structures , 1987, Biopolymers.
[15] J. Ponder,et al. Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. , 1987, Journal of molecular biology.
[16] A. Lesk,et al. Canonical structures for the hypervariable regions of immunoglobulins. , 1987, Journal of molecular biology.
[17] M. Karplus,et al. Prediction of the folding of short polypeptide segments by uniform conformational sampling , 1987, Biopolymers.
[18] J. Thornton,et al. Analysis and prediction of the different types of β-turn in proteins , 1988 .
[19] R. Bruccoleri,et al. Criteria that discriminate between native proteins and incorrectly folded models , 1988, Proteins.
[20] C. Goodman,et al. Fasciclin III: A novel homophilic adhesion molecule in Drosophila , 1989, Cell.
[21] C Sander,et al. Polarity as a criterion in protein design. , 1989, Protein engineering.
[22] N. D. Clarke,et al. Identification of protein folds: Matching hydrophobicity patterns of sequence sets with solvent accessibility patterns of known structures , 1990, Proteins.
[23] F E Cohen,et al. Novel method for the rapid evaluation of packing in protein structures. , 1990, Journal of molecular biology.
[24] F E Cohen,et al. Protein model structure evaluation using the solvation free energy of folding. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[25] K. Dill,et al. Theory for protein mutability and biogenesis. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[26] G. Casari,et al. Identification of native protein folds amongst a large number of incorrect models. The calculation of low energy conformations from potentials of mean force. , 1990, Journal of molecular biology.
[27] N. Patel,et al. Molecular genetics of neuronal recognition in Drosophila: evolution and function of immunoglobulin superfamily cell adhesion molecules. , 1990, Cold Spring Harbor symposia on quantitative biology.
[28] M. Sippl. Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge-based prediction of local structures in globular proteins. , 1990, Journal of molecular biology.
[29] C. Sander,et al. Database algorithm for generating protein backbone and side-chain co-ordinates from a C alpha trace application to model building and detection of co-ordinate errors. , 1991, Journal of molecular biology.
[30] A. D. McLachlan,et al. Secondary structure‐based profiles: Use of structure‐conserving scoring tables in searching protein sequence databases for structural similarities , 1991, Proteins.
[31] G. Crippen. Prediction of protein folding from amino acid sequence over discrete conformation spaces. , 1991, Biochemistry.
[32] K. Sharp,et al. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons , 1991, Proteins.
[33] H. Scheraga,et al. Empirical solvation models can be used to differentiate native from near‐native conformations of bovine pancreatic trypsin inhibitor , 1991, Proteins.
[34] J. Greer,et al. Comparative modeling of homologous proteins. , 1991, Methods in enzymology.
[35] S F Altschul,et al. Statistical methods and insights for protein and DNA sequences. , 1991, Annual review of biophysics and biophysical chemistry.
[36] M. Sippl,et al. Detection of native‐like models for amino acid sequences of unknown three‐dimensional structure in a data base of known protein conformations , 1992, Proteins.
[37] C. Sander,et al. Fast and simple monte carlo algorithm for side chain optimization in proteins: Application to model building by homology , 1992, Proteins.
[38] D. Eisenberg,et al. Assessment of protein models with three-dimensional profiles , 1992, Nature.
[39] Harold A. Scheraga,et al. Standard‐geometry chains fitted to X‐ray derived structures: Validation of the rigid‐geometry approximation. II. Systematic searches for short loops in proteins: Applications to bovine pancreatic ribonuclease A and human lysozyme , 1992 .
[40] John P. Overington,et al. Environment‐specific amino acid substitution tables: Tertiary templates and prediction of protein folds , 1992, Protein science : a publication of the Protein Society.
[41] D. T. Jones,et al. A new approach to protein fold recognition , 1992, Nature.
[42] C. Chothia. One thousand families for the molecular biologist , 1992, Nature.
[43] G. Crippen,et al. Contact potential that recognizes the correct folding of globular proteins. , 1992, Journal of molecular biology.
[44] Johan Desmet,et al. The dead-end elimination theorem and its use in protein side-chain positioning , 1992, Nature.
[45] F. Cohen,et al. Taxonomy and conformational analysis of loops in proteins. , 1992, Journal of molecular biology.
[46] C. Sander,et al. Evaluation of protein models by atomic solvation preference. , 1992, Journal of molecular biology.
[47] A. Godzik,et al. Topology fingerprint approach to the inverse protein folding problem. , 1992, Journal of molecular biology.
[48] S. Bryant,et al. An empirical energy function for threading protein sequence through the folding motif , 1993, Proteins.