The native state conformational ensemble of the SH3 domain from alpha-spectrin.
about
Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissuesThe high-resolution NMR structure of the R21A Spc-SH3:P41 complex: Understanding the determinants of binding affinity by comparison with Abl-SH3Role of Interfacial Water Molecules in Proline-rich Ligand Recognition by the Src Homology 3 Domain of AblFrom Binding-Induced Dynamic Effects in SH3 Structures to Evolutionary Conserved SectorsMapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis.Modulation of the stability of amyloidogenic precursors by anion binding strongly influences the rate of amyloid nucleation.Characterization of oligomers of heterogeneous size as precursors of amyloid fibril nucleation of an SH3 domain: an experimental kinetics study.Interfacial water molecules in SH3 interactions: Getting the full picture on polyproline recognition by protein-protein interaction domains.Interfacial water molecules in SH3 interactions: a revised paradigm for polyproline recognition.NMR-based conformational ensembles explain pH-gated opening and closing of OmpG channel.Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP.Environmental conditions affect the kinetics of nucleation of amyloid fibrils and determine their morphology.Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration.A single mutation in an SH3 domain increases amyloid aggregation by accelerating nucleation, but not by destabilizing thermodynamically the native state.Detection and characterization of partially unfolded oligomers of the SH3 domain of alpha-spectrin.A binding event converted into a folding event.Structural cooperativity in the SH3 domain studied by site-directed mutagenesis and amide hydrogen exchange.The temperature dependence of the hydrogen exchange in the SH3 domain of alpha-spectrin.pH dependence of the hydrogen exchange in the SH3 domain of alpha-spectrin.Thermodynamic propensities of amino acids in the native state ensemble: implications for fold recognition.The folding energy landscape of apoflavodoxin is rugged: hydrogen exchange reveals nonproductive misfolded intermediatesHydrogen-exchange stability analysis of Bergerac-Src homology 3 variants allows the characterization of a folding intermediate in equilibriumThe propagation of binding interactions to remote sites in proteins: analysis of the binding of the monoclonal antibody D1.3 to lysozymeCan allosteric regulation be predicted from structure?Three-dimensional structure determines the pattern of CD4+ T-cell epitope dominance in influenza virus hemagglutinin.Evidence for conformational heterogeneity of fission protein Fis1 from Saccharomyces cerevisiae.Comparative NMR study on the impact of point mutations on protein stability of Pseudomonas mendocina lipase.Hydrogen exchange of the tetramerization domain of the human tumour suppressor p53 probed by denaturants and temperature.
P2860
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P2860
The native state conformational ensemble of the SH3 domain from alpha-spectrin.
description
1999 nî lūn-bûn
@nan
1999 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The native state conformational ensemble of the SH3 domain from alpha-spectrin.
@ast
The native state conformational ensemble of the SH3 domain from alpha-spectrin.
@en
type
label
The native state conformational ensemble of the SH3 domain from alpha-spectrin.
@ast
The native state conformational ensemble of the SH3 domain from alpha-spectrin.
@en
prefLabel
The native state conformational ensemble of the SH3 domain from alpha-spectrin.
@ast
The native state conformational ensemble of the SH3 domain from alpha-spectrin.
@en
P2093
P356
P1433
P1476
The native state conformational ensemble of the SH3 domain from alpha-spectrin.
@en
P2093
Conejero-Lara F
López-Mayorga O
P304
P356
10.1021/BI990413G
P407
P577
1999-07-01T00:00:00Z