Side-chain conformational entropy at protein-protein interfaces.
about
On side-chain conformational entropy of proteinsThermodynamically reengineering the listerial invasion complex InlA/E-cadherinDesigned protein-protein associationLoss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculationsProgress and challenges in predicting protein interfacesAlgorithmic approaches to protein-protein interaction site prediction.Common physical basis of macromolecule-binding sites in proteinsInferring the microscopic surface energy of protein-protein interfaces from mutation data.Mechanisms for stabilisation and the maintenance of solubility in proteins from thermophiles.Improving the prediction of protein binding sites by combining heterogeneous data and Voronoi diagrams.Role of anisotropic interactions for proteins and patchy nanoparticles.Protein binding site prediction using an empirical scoring functionProtein-protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfacesComputational Tools for Interpreting Ion Channel pH-Dependence.Progress in the prediction of pKa values in proteinsInsights into the quaternary association of proteins through structure graphs: a case study of lectins.A Gradient of Sitewise Diversity Promotes Evolutionary Fitness for Binder Discovery in a Three-Helix Bundle Protein Scaffold.Entropic contributions and the influence of the hydrophobic environment in promiscuous protein-protein associationInteraction-site prediction for protein complexes: a critical assessment.Lysine and arginine content of proteins: computational analysis suggests a new tool for solubility design.Redesigning protein cavities as a strategy for increasing affinity in protein-protein interaction: interferon- γ receptor 1 as a model.Volume-based solvation models out-perform area-based models in combined studies of wild-type and mutated protein-protein interfaces.Are protein-protein interfaces more conserved in sequence than the rest of the protein surface?Computer-aided design and discovery of protein-protein interaction inhibitors as agents for anti-HIV therapy.pKa predictions with a coupled finite difference Poisson-Boltzmann and Debye-Hückel method.Protein-protein interactions in paralogues: Electrostatics modulates specificity on a conserved steric scaffold.Improved pKa calculations through flexibility based sampling of a water-dominated interaction scheme.Prediction of pKa and redox properties in the thioredoxin superfamily.Soluble expression of proteins correlates with a lack of positively-charged surface.Local and global anatomy of antibody-protein antigen recognition.
P2860
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P2860
Side-chain conformational entropy at protein-protein interfaces.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
Side-chain conformational entropy at protein-protein interfaces.
@en
type
label
Side-chain conformational entropy at protein-protein interfaces.
@en
prefLabel
Side-chain conformational entropy at protein-protein interfaces.
@en
P2860
P356
P1433
P1476
Side-chain conformational entropy at protein-protein interfaces
@en
P2093
Christian Cole
Jim Warwicker
P2860
P304
P356
10.1110/PS.0222702
P577
2002-12-01T00:00:00Z