From residue coevolution to protein conformational ensembles and functional dynamics.
about
Potts Hamiltonian models of protein co-variation, free energy landscapes, and evolutionary fitness.Improving landscape inference by integrating heterogeneous data in the inverse Ising problem.Inference of Epistatic Effects Leading to Entrenchment and Drug Resistance in HIV-1 Protease.New Techniques for Ancient Proteins: Direct Coupling Analysis Applied on Proteins Involved in Iron Sulfur Cluster BiogenesisACE: adaptive cluster expansion for maximum entropy graphical model inference.Computational Analysis of Residue Interaction Networks and Coevolutionary Relationships in the Hsp70 Chaperones: A Community-Hopping Model of Allosteric Regulation and CommunicationInferring repeat-protein energetics from evolutionary information.The Gearbox of the Bacterial Flagellar Motor Switch.Connecting the Sequence-Space of Bacterial Signaling Proteins to Phenotypes Using Coevolutionary Landscapes.Conservation of coevolving protein interfaces bridges prokaryote-eukaryote homologies in the twilight zone.Epistasis in protein evolution.Large-scale identification of coevolution signals across homo-oligomeric protein interfaces by direct coupling analysis.Correlated positions in protein evolution and engineering.Widespread Historical Contingency in Influenza Viruses.Direct coevolutionary couplings reflect biophysical residue interactions in proteins.Structural propensities of kinase family proteins from a Potts model of residue co-variation.Co-evolution techniques are reshaping the way we do structural bioinformatics.Monte Carlo simulation of a statistical mechanical model of multiple protein sequence alignment.Origins of coevolution between residues distant in protein 3D structures.Enhanced unbiased sampling of protein dynamics using evolutionary coupling information.Structural, physicochemical and dynamic features conserved within the aerolysin pore-forming toxin family.Assessment of the model refinement category in CASP12.Coevolutionary Landscape of Kinase Family Proteins: Sequence Probabilities and Functional Motifs.Patterns of coevolving amino acids unveil structural and dynamical domains.Inferring joint sequence-structural determinants of protein functional specificity.Biomolecular coevolution and its applications: Going from structure prediction toward signaling, epistasis, and function.Characterization of C-ring component assembly in flagellar motors from amino acid coevolution.Widespread evolutionary crosstalk among protein domains in the context of multi-domain proteins
P2860
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P2860
From residue coevolution to protein conformational ensembles and functional dynamics.
description
2015 nî lūn-bûn
@nan
2015 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
From residue coevolution to protein conformational ensembles and functional dynamics
@nl
From residue coevolution to protein conformational ensembles and functional dynamics.
@ast
From residue coevolution to protein conformational ensembles and functional dynamics.
@en
type
label
From residue coevolution to protein conformational ensembles and functional dynamics
@nl
From residue coevolution to protein conformational ensembles and functional dynamics.
@ast
From residue coevolution to protein conformational ensembles and functional dynamics.
@en
prefLabel
From residue coevolution to protein conformational ensembles and functional dynamics
@nl
From residue coevolution to protein conformational ensembles and functional dynamics.
@ast
From residue coevolution to protein conformational ensembles and functional dynamics.
@en
P2860
P50
P3181
P356
P1476
From residue coevolution to protein conformational ensembles and functional dynamics.
@en
P2860
P304
13567-13572
P3181
P356
10.1073/PNAS.1508584112
P407
P577
2015-10-20T00:00:00Z