A stability pattern of protein hydrophobic mutations that reflects evolutionary structural optimization.
about
Selection for Protein Kinetic Stability Connects Denaturation Temperatures to Organismal Temperatures and Provides Clues to Archaean LifeInferring stabilizing mutations from protein phylogenies: application to influenza hemagglutinin.Role of conservative mutations in protein multi-property adaptationStabilizing proteins from sequence statistics: the interplay of conservation and correlation in triosephosphate isomerase stability.Mutational studies on resurrected ancestral proteins reveal conservation of site-specific amino acid preferences throughout evolutionary history.Contribution of charged groups to the enthalpic stabilization of the folded states of globular proteins.Enhanced vulnerability of human proteins towards disease-associated inactivation through divergent evolution.Making sense of the past: hyperstability of ancestral thioredoxins explained by free energy simulations.
P2860
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P2860
A stability pattern of protein hydrophobic mutations that reflects evolutionary structural optimization.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
A stability pattern of protein ...... onary structural optimization.
@en
A stability pattern of protein ...... onary structural optimization.
@nl
type
label
A stability pattern of protein ...... onary structural optimization.
@en
A stability pattern of protein ...... onary structural optimization.
@nl
prefLabel
A stability pattern of protein ...... onary structural optimization.
@en
A stability pattern of protein ...... onary structural optimization.
@nl
P2093
P2860
P1433
P1476
A stability pattern of protein ...... ionary structural optimization
@en
P2093
Beatriz Ibarra-Molero
Raquel Godoy-Ruiz
Raul Perez-Jimenez
P2860
P304
P356
10.1529/BIOPHYSJ.105.067025
P407
P577
2005-08-12T00:00:00Z