Modeling coding-sequence evolution within the context of residue solvent accessibility.
about
Causes of evolutionary rate variation among protein sitesFunctional Sites Induce Long-Range Evolutionary Constraints in EnzymesAmino-acid site variability among natural and designed proteinsPredicting evolutionary site variability from structure in viral proteins: buriedness, packing, flexibility, and design.Roles of solvent accessibility and gene expression in modeling protein sequence evolutionThe utility of protein structure as a predictor of site-wise dN/dS varies widely among HIV-1 proteins.Dissecting the roles of local packing density and longer-range effects in protein sequence evolutionBiophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence.Integrating sequence variation and protein structure to identify sites under selectionIndependent effects of protein core size and expression on residue-level structure-evolution relationships.Cross-species comparison of site-specific evolutionary-rate variation in influenza haemagglutinin.Local packing density is the main structural determinant of the rate of protein sequence evolution at site level.An experimentally informed evolutionary model improves phylogenetic fit to divergent lactamase homologsBiophysics of protein evolution and evolutionary protein biophysicsMaximum allowed solvent accessibilites of residues in proteinsThe relationship between dN/dS and scaled selection coefficients.Universal distribution of mutational effects on protein stability, uncoupling of protein robustness from sequence evolution and distinct evolutionary modes of prokaryotic and eukaryotic proteins.Calculating site-specific evolutionary rates at the amino-acid or codon level yields similar rate estimates.Intermediate divergence levels maximize the strength of structure-sequence correlations in enzymes and viral proteins.Measuring evolutionary rates of proteins in a structural context.Substitution rates predicted by stability-constrained models of protein evolution are not consistent with empirical data.Differential strengths of molecular determinants guide environment specific mutational fates.Influence of mutation bias and hydrophobicity on the substitution rates and sequence entropies of protein evolution
P2860
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P2860
Modeling coding-sequence evolution within the context of residue solvent accessibility.
description
2012 nî lūn-bûn
@nan
2012 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Modeling coding-sequence evolution within the context of residue solvent accessibility.
@ast
Modeling coding-sequence evolution within the context of residue solvent accessibility.
@en
type
label
Modeling coding-sequence evolution within the context of residue solvent accessibility.
@ast
Modeling coding-sequence evolution within the context of residue solvent accessibility.
@en
prefLabel
Modeling coding-sequence evolution within the context of residue solvent accessibility.
@ast
Modeling coding-sequence evolution within the context of residue solvent accessibility.
@en
P2860
P356
P1476
Modeling coding-sequence evolution within the context of residue solvent accessibility.
@en
P2093
Michael P Scherrer
P2860
P2888
P356
10.1186/1471-2148-12-179
P577
2012-09-12T00:00:00Z
P5875
P6179
1030776348