Short-range conformational energies, secondary structure propensities, and recognition of correct sequence-structure matches

scientific article published on November 1, 1997

Short-range conformational energies, secondary structure propensities, and recognition of correct sequence-structure matches is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1002/(SICI)1097-0134(199711)29:3<292::AID-PROT4>3.3.CO;2-5
10.1002/(SICI)1097-0134(199711)29:3<292::AID-PROT4>3.0.CO;2-D
P953full work available at URLhttps://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2F(SICI)1097-0134(199711)29:3%3C292::AID-PROT4%3E3.0.CO;2-D
https://onlinelibrary.wiley.com/doi/full/10.1002/(SICI)1097-0134(199711)29:3%3C292::AID-PROT4%3E3.0.CO;2-D
P698PubMed publication ID9365985

P50authorRobert L JerniganQ59682925
P2093author name stringM. Kaplan
I. Bahar
P2860cites workInter-residue potentials in globular proteins and the dominance of highly specific hydrophilic interactions at close separationQ47627928
Factors influencing the ability of knowledge-based potentials to identify native sequence-structure matchesQ47633923
Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threadingQ52310162
Elucidating the folding problem of helical peptides using empirical parametersQ52376869
A thermodynamic scale for the beta-sheet forming tendencies of the amino acidsQ53709834
Thermodynamic beta-sheet propensities measured using a zinc-finger host peptideQ54269563
Side-Chain Determinants of .beta.-Sheet StabilityQ57823374
Context-dependent secondary structure formation of a designed protein sequenceQ59055217
Measurement of the β-sheet-forming propensities of amino acidsQ59069627
Context is a major determinant of β-sheet propensityQ59069633
Positional independence and additivity of amino acid replacements on helix stability in monomeric peptidesQ67290878
Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfacesQ67559626
Identification of native protein folds amongst a large number of incorrect models. The calculation of low energy conformations from potentials of mean forceQ68363646
Side chain contributions to the stability of alpha-helical structure in peptidesQ68598333
A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helixQ68754537
Structure-based thermodynamic scale of alpha-helix propensities in amino acidsQ71714553
Importance of environment in determining secondary structure in proteinsQ72266480
Hydrogen bond strength and beta-sheet propensities: the role of a side chain blocking effectQ72511006
Development of pseudoenergy potentials for assessing protein 3-D-1-D compatibility and detecting weak homologiesQ72777487
Structural basis of amino acid alpha helix propensityQ27732169
Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteinsQ27860987
The Protein Data Bank: a computer-based archival file for macromolecular structuresQ27860989
A simplified representation of protein conformations for rapid simulation of protein foldingQ28269973
Energy functions that discriminate X-ray and near native folds from well-constructed decoysQ28278562
Amino acid preferences for specific locations at the ends of alpha helicesQ29618508
The complexity and accuracy of discrete state models of protein structureQ30418649
Reduced representation model of protein structure prediction: statistical potential and genetic algorithmsQ30422972
Coordination geometry of nonbonded residues in globular proteinsQ33368037
Side-chain entropy opposes alpha-helix formation but rationalizes experimentally determined helix-forming propensitiesQ33611710
Knowledge-based prediction of protein structures and the design of novel moleculesQ34183412
Rules for alpha-helix termination by glycineQ34340813
Stabilization of lambda repressor against thermal denaturation by site-directed Gly----Ala changes in alpha-helix 3.Q38350564
Adding backbone to protein folding: why proteins are polypeptidesQ41394310
Alpha-helix stability in proteins. II. Factors that influence stability at an internal positionQ41949296
Pseudodihedrals: simplified protein backbone representation with knowledge-based energyQ42844377
Amino acid similarity coefficients for protein modeling and sequence alignment derived from main-chain folding anglesQ43994343
A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acidsQ44211659
Conformational preferences of amino acids in globular proteinsQ44870543
Relative helix-forming tendencies of nonpolar amino acidsQ46587484
Protein folding. Effect of packing density on chain conformationQ46927963
P433issue3
P407language of work or nameEnglishQ1860
P921main subjectcomputational scienceQ117801
protein secondary structureQ904984
P304page(s)292-308
P577publication date1997-11-01
P1433published inProteinsQ7251514
P1476titleShort-range conformational energies, secondary structure propensities, and recognition of correct sequence-structure matches
P478volume29

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