Empirical scale of side-chain conformational entropy in protein folding.
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On side-chain conformational entropy of proteinsInteratomic potentials and solvation parameters from protein engineering data for buried residuesQuantification of helix-helix binding affinities in micelles and lipid bilayersEntropic stabilization of proteins and its proteomic consequencesExperimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymesContribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozymeA small engineered protein lacks structural uniqueness by increasing the side-chain conformational entropyEfficient Computation of Small-Molecule Configurational Binding Entropy and Free Energy Changes by Ensemble EnumerationFolding of proteins with an all-atom Go-model.Selecting near-native conformations in homology modeling: the role of molecular mechanics and solvation termsFree energy determinants of tertiary structure and the evaluation of protein models.Flexible mapping of homology onto structure with homolmapper.Geofold: topology-based protein unfolding pathways capture the effects of engineered disulfides on kinetic stability.Principles of protein folding--a perspective from simple exact models.Effects of salt bridges on protein structure and design.Toward rational protein crystallization: A Web server for the design of crystallizable protein variants.A linkage analysis toolkit for studying allosteric networks in ion channels.Molecular basis for the Cu2+ binding-induced destabilization of beta2-microglobulin revealed by molecular dynamics simulation.Exploring the conformational space of protein side chains using dead-end elimination and the A* algorithm.Side-chain entropy and packing in proteins.Protein side-chain dynamics and residual conformational entropyDefining the functional domain of programmed cell death 10 through its interactions with phosphatidylinositol-3,4,5-trisphosphate.Enhanced crystal packing due to solvent reorganization through reductive methylation of lysine residues in oxidoreductase from Streptococcus pneumoniae.Electrostatic contributions to the binding free energy of the lambdacI repressor to DNA.Free energy decomposition of protein-protein interactions.A directed essential dynamics simulation of peptide folding.Relative free energy of binding between antimicrobial peptides and SDS or DPC micelles.Correlation analysis of the side-chains conformational distribution in bound and unbound proteins.Side-chain conformational entropy in protein foldingSCMCRYS: predicting protein crystallization using an ensemble scoring card method with estimating propensity scores of P-collocated amino acid pairs.Functional and dysfunctional conformers of human neuroserpin characterized by optical spectroscopies and Molecular DynamicsLigand configurational entropy and protein binding.Structure-based prediction of the stability of transmembrane helix-helix interactions: the sequence dependence of glycophorin A dimerizationEffect of the Crystal Environment on Side-Chain Conformational Dynamics in Cyanovirin-N Investigated through Crystal and Solution Molecular Dynamics Simulations.Discovering structural correlations in alpha-helices.Empirical free energy calculation: comparison to calorimetric data.Thermal stability of hydrophobic heme pocket variants of oxidized cytochrome cAn improved experimental system for determining small folding entropy changes resulting from proline to alanine substitutionsElectrostatic properties of cowpea chlorotic mottle virus and cucumber mosaic virus capsidsFree energy of burying hydrophobic residues in the interface between protein subunits.
P2860
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P2860
Empirical scale of side-chain conformational entropy in protein folding.
description
1993 nî lūn-bûn
@nan
1993 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Empirical scale of side-chain conformational entropy in protein folding.
@ast
Empirical scale of side-chain conformational entropy in protein folding.
@en
Empirical scale of side-chain conformational entropy in protein folding.
@nl
type
label
Empirical scale of side-chain conformational entropy in protein folding.
@ast
Empirical scale of side-chain conformational entropy in protein folding.
@en
Empirical scale of side-chain conformational entropy in protein folding.
@nl
prefLabel
Empirical scale of side-chain conformational entropy in protein folding.
@ast
Empirical scale of side-chain conformational entropy in protein folding.
@en
Empirical scale of side-chain conformational entropy in protein folding.
@nl
P356
P1476
Empirical scale of side-chain conformational entropy in protein folding.
@en
P2093
Pickett SD
Sternberg MJ
P304
P356
10.1006/JMBI.1993.1329
P407
P577
1993-06-01T00:00:00Z