Sequence entropy of folding and the absolute rate of amino acid substitutions.
about
Substitution rates predicted by stability-constrained models of protein evolution are not consistent with empirical data.Influence of mutation bias and hydrophobicity on the substitution rates and sequence entropies of protein evolutionFunctional trade-offs and environmental variation shaped ancient trajectories in the evolution of dim-light visionModeling site-specific amino-acid preferences deepens phylogenetic estimates of viral sequence divergenceSelection for Protein Stability Enriches for Epistatic Interactions
P2860
Sequence entropy of folding and the absolute rate of amino acid substitutions.
description
2017 nî lūn-bûn
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2017年の論文
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2017年学术文章
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2017年学术文章
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2017年学术文章
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2017年学术文章
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2017年学术文章
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2017年学术文章
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2017年學術文章
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2017年學術文章
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name
Sequence entropy of folding and the absolute rate of amino acid substitutions.
@en
Sequence entropy of folding and the absolute rate of amino acid substitutions.
@nl
type
label
Sequence entropy of folding and the absolute rate of amino acid substitutions.
@en
Sequence entropy of folding and the absolute rate of amino acid substitutions.
@nl
prefLabel
Sequence entropy of folding and the absolute rate of amino acid substitutions.
@en
Sequence entropy of folding and the absolute rate of amino acid substitutions.
@nl
P2860
P1476
Sequence entropy of folding and the absolute rate of amino acid substitutions.
@en
P2860
P2888
P304
P356
10.1038/S41559-017-0338-9
P577
2017-10-23T00:00:00Z