Engineering Protein Allostery: 1.05 Å Resolution Structure and Enzymatic Properties of a Na+-activated Trypsin
about
Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin FoldQuantifying Correlations Between Allosteric Sites in Thermodynamic EnsemblesRigid Residue Scan Simulations Systematically Reveal Residue Entropic Roles in Protein AllosteryRedesigning allosteric activation in an enzyme.Functional identification and characterization of sodium binding sites in Na symporters.Proteases as therapeutics.Integrative systems and synthetic biology of cell-matrix adhesion sites.Molecular Mechanisms of Enzyme Activation by Monovalent Cations.Exploring modular allostery via interchangeable regulatory domains.Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site.
P2860
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P2860
Engineering Protein Allostery: 1.05 Å Resolution Structure and Enzymatic Properties of a Na+-activated Trypsin
description
2008 nî lūn-bûn
@nan
2008 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Engineering Protein Allostery: ...... ies of a Na+-activated Trypsin
@ast
Engineering Protein Allostery: ...... ies of a Na+-activated Trypsin
@en
Engineering Protein Allostery: ...... ies of a Na+-activated Trypsin
@nl
type
label
Engineering Protein Allostery: ...... ies of a Na+-activated Trypsin
@ast
Engineering Protein Allostery: ...... ies of a Na+-activated Trypsin
@en
Engineering Protein Allostery: ...... ies of a Na+-activated Trypsin
@nl
prefLabel
Engineering Protein Allostery: ...... ies of a Na+-activated Trypsin
@ast
Engineering Protein Allostery: ...... ies of a Na+-activated Trypsin
@en
Engineering Protein Allostery: ...... ies of a Na+-activated Trypsin
@nl
P2093
P2860
P3181
P1476
Engineering Protein Allostery: ...... ies of a Na+-activated Trypsin
@en
P2093
Christopher J Carrell
Enrico Di Cera
Michael J Page
P2860
P304
P3181
P356
10.1016/J.JMB.2008.03.003
P407
P577
2008-05-02T00:00:00Z