Prediction of protein backbone conformation based on seven structure assignments. Influence of local interactions.

[1]  T. Creighton,et al.  Protein Folding , 1992 .

[2]  S J Wodak,et al.  Sesam: A relational database for structure and sequence of macromolecules , 1991, Proteins.

[3]  J. Gibrat,et al.  Influence of the local amino acid sequence upon the zones of the torsional angles phi and psi adopted by residues in proteins. , 1991, Biochemistry.

[4]  M J Rooman,et al.  Weak correlation between predictive power of individual sequence patterns and overall prediction accuracy in proteins , 1991, Proteins.

[5]  P E Wright,et al.  Structural characterization of a partly folded apomyoglobin intermediate. , 1990, Science.

[6]  E. Stellwagen,et al.  Effect of central-residue replacements on the helical stability of a monomeric peptide. , 1990, Biochemistry.

[7]  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.

[8]  S. Wodak,et al.  Relations between protein sequence and structure and their significance. , 1990, Journal of molecular biology.

[9]  J. Thornton,et al.  Beta-turns and their distortions: a proposed new nomenclature. , 1990, Protein engineering.

[10]  A Kolinski,et al.  Dynamic Monte Carlo simulations of globular protein folding/unfolding pathways. I. Six-member, Greek key beta-barrel proteins. , 1990, Journal of molecular biology.

[11]  Robert L. Baldwin,et al.  Relative helix-forming tendencies of nonpolar amino acids , 1990, Nature.

[12]  E. Stellwagen,et al.  Positional independence and additivity of amino acid replacements on helix stability in monomeric peptides. , 1990, Biochemistry.

[13]  A. V. Finkelstein,et al.  Theory of cooperative transitions in protein molecules. II. Phase diagram for a protein molecule in solution , 1989, Biopolymers.

[14]  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.

[15]  A. Fersht,et al.  Mapping the transition state and pathway of protein folding by protein engineering , 1989, Nature.

[16]  R. L. Baldwin,et al.  Unusually stable helix formation in short alanine-based peptides. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[17]  E. Stellwagen,et al.  Analysis of peptides for helical prediction. , 1989, Biochemistry.

[18]  C M Dobson,et al.  Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin. , 1989, Biochemistry.

[19]  Alexey G. Murzin,et al.  General architecture of the α-helical globule , 1988 .

[20]  S. Suhai,et al.  Secondary structure of the Arg-Gly-Asp recognition site in proteins involved in cell-surface adhesion. Evidence for the occurrence of nested beta-bends in the model hexapeptide GRGDSP. , 1988, European journal of biochemistry.

[21]  Terrence G. Oas,et al.  A peptide model of a protein folding intermediate , 1988, Nature.

[22]  S. Walter Englander,et al.  Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR , 1988, Nature.

[23]  Robert L. Baldwin,et al.  NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A , 1988, Nature.

[24]  P E Wright,et al.  Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding. , 1988, Biochemistry.

[25]  Shoshana J. Wodak,et al.  Identification of predictive sequence motifs limited by protein structure data base size , 1988, Nature.

[26]  H. Drobecq,et al.  Influence of helical organization on immunogenicity and antigenicity of synthetic peptides. , 1988, Molecular immunology.

[27]  J. Richardson,et al.  Amino acid preferences for specific locations at the ends of alpha helices. , 1988, Science.

[28]  G. Rose,et al.  Helix signals in proteins. , 1988, Science.

[29]  P. Gooley,et al.  Location of an alpha-helix in fragment 96-133 from bovine somatotropin by 1H NMR spectroscopy. , 1988, Biochemistry.

[30]  P E Wright,et al.  Folding of immunogenic peptide fragments of proteins in water solution. I. Sequence requirements for the formation of a reverse turn. , 1988, Journal of molecular biology.

[31]  P E Wright,et al.  Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix. , 1988, Journal of molecular biology.

[32]  J. Gibrat,et al.  Further developments of protein secondary structure prediction using information theory. New parameters and consideration of residue pairs. , 1987, Journal of molecular biology.

[33]  R. L. Baldwin,et al.  Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[34]  E. W. Kauffman,et al.  Helical formation in isolated fragments of bovine growth hormone. , 1987, Biochemistry.

[35]  H. Scheraga,et al.  Monte Carlo-minimization approach to the multiple-minima problem in protein folding. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[36]  M. Jiménez,et al.  1H NMR and CD evidence of the folding of the isolated ribonuclease 50–61 fragment , 1987, FEBS letters.

[37]  O. Ptitsyn.  Protein folding: Hypotheses and experiments , 1987 .

[38]  H A Scheraga,et al.  Prediction of the native conformation of a polypeptide by a statistical‐mechanical procedure. III. Probable and average conformations of enkephalin , 1987, Biopolymers.

[39]  Robert L. Baldwin,et al.  Tests of the helix dipole model for stabilization of α-helices , 1987, Nature.

[40]  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.

[41]  J. Moult,et al.  An algorithm for determining the conformation of polypeptide segments in proteins by systematic search , 1986, Proteins.

[42]  D Eisenberg,et al.  The design, synthesis, and crystallization of an alpha‐helical peptide , 1986, Proteins.

[43]  R. Lerner,et al.  The immunodominant site of a synthetic immunogen has a conformational preference in water for a type-II reverse turn , 1985, Nature.

[44]  R. Jernigan,et al.  Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation , 1985 .

[45]  P. S. Kim,et al.  Nature of the charged-group effect on the stability of the C-peptide helix. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[46]  H. Scheraga,et al.  Chain-folding initiation structures in ribonuclease A: conformational analysis of trans-Ac-Asn-Pro-Tyr-NHMe and trans-Ac-Tyr-Pro-Asn-NHMe in water and in the solid state , 1984 .

[47]  A M Lesk,et al.  Mechanisms of domain closure in proteins. , 1984, Journal of molecular biology.

[48]  C Sander,et al.  On the use of sequence homologies to predict protein structure: identical pentapeptides can have completely different conformations. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[49]  W. Kabsch,et al.  Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.

[50]  C. D. Gelatt,et al.  Optimization by Simulated Annealing , 1983, Science.

[51]  W. Kabsch,et al.  How good are predictions of protein secondary structure? , 1983, FEBS letters.

[52]  R. Jernigan,et al.  Equilibrium folding and unfolding pathways for a model protein , 1982, Biopolymers.

[53]  P. S. Kim,et al.  A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A. , 1982, Proceedings of the National Academy of Sciences of the United States of America.

[54]  O. B. Ptitsyn,et al.  Protein folding: general physical model , 1981 .

[55]  K. Hallenga,et al.  The conformational properties of the peptide hormone somatostatin (III) , 1980, FEBS letters.

[56]  F E Cohen,et al.  Protein folding: evaluation of some simple rules for the assembly of helices into tertiary structures with myoglobin as an example. , 1979, Journal of molecular biology.

[57]  Hans Frauenfelder,et al.  Temperature-dependent X-ray diffraction as a probe of protein structural dynamics , 1979, Nature.

[58]  K. Hallenga,et al.  The conformational properties of some fragments of the peptide hormone somatostatin. , 1979, Biochimica et biophysica acta.

[59]  W. Kabsch.  A discussion of the solution for the best rotation to relate two sets of vectors , 1978 .

[60]  N. Go,et al.  Studies on protein folding, unfolding, and fluctuations by computer simulation. II. A. Three‐dimensional lattice model of lysozyme , 1978 .

[61]  J. Garnier,et al.  Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. , 1978, Journal of molecular biology.

[62]  G J Williams,et al.  The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.

[63]  V. Hruby,et al.  Relative conformational rigidity in oxytocin and (1-penicillamine)-oxytocin: a proposal for the relationship of conformational flexibility to peptide hormone agonism and antagonism. , 1977, Proceedings of the National Academy of Sciences of the United States of America.

[64]  M. Levitt.  A simplified representation of protein conformations for rapid simulation of protein folding. , 1976, Journal of molecular biology.

[65]  E. Ralston,et al.  Folding of polypeptide chains induced by the amino acid side-chains. , 1974, Journal of molecular biology.

[66]  H. Scheraga.  Theoretical and experimental studies of conformations of polypeptides. , 1971, Chemical reviews.

[67]  J. E. Brown,et al.  Helix-coil transition of the isolated amino terminus of ribonuclease. , 1971, Biochemistry.

[68]  A. M. Liquori.  The stereochemical code and the logic of a protein molecule , 1969, Quarterly Reviews of Biophysics.

[69]  J. Gibrat,et al.  Secondary structure prediction and protein design. , 1990, Biochemical Society symposium.

[70]  J. Skolnick,et al.  Computer simulations of globular protein folding and tertiary structure. , 1989, Annual review of physical chemistry.

[71]  G. Fasman.  The Development of the Prediction of Protein Structure , 1989 .

[72]  S. Doniach,et al.  A computer model to dynamically simulate protein folding: Studies with crambin , 1989, Proteins.

[73]  G. Schulz,et al.  A critical evaluation of methods for prediction of protein secondary structures. , 1988, Annual review of biophysics and biophysical chemistry.

[74]  G A Petsko,et al.  Fluctuations in protein structure from X-ray diffraction. , 1984, Annual review of biophysics and bioengineering.

[75]  P. S. Kim,et al.  Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. , 1982, Annual review of biochemistry.

[76]  G. N. Ramachandran,et al.  Conformation of polypeptides and proteins. , 1968, Advances in protein chemistry.