NMR evidence for forming highly populated helical conformations in the partially folded hNck2 SH3 domain.
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Insights into protein aggregation by NMR characterization of insoluble SH3 mutants solubilized in salt-free waterNMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional DynamicsStructural study of hNck2 SH3 domain protein in solution by circular dichroism and X-ray solution scattering.VAPC, an human endogenous inhibitor for hepatitis C virus (HCV) infection, is intrinsically unstructured but forms a "fuzzy complex" with HCV NS5B.Amphiphilic α-helical potential: a putative folding motif adding few constraints to protein evolution.Insight into "insoluble proteins" with pure water.Unique structure and dynamics of the EphA5 ligand binding domain mediate its binding specificity as revealed by X-ray crystallography, NMR and MD simulationsWhy do proteins aggregate? "Intrinsically insoluble proteins" and "dark mediators" revealed by studies on "insoluble proteins" solubilized in pure water.
P2860
Q28471978-3F19214C-09C8-4F9B-BA44-B8743863E543Q28547136-5BB58192-8EE0-47DF-837C-59DE9F82208FQ30009895-6A8520E8-BBF9-4FFC-8952-DD6976E87AD7Q30155273-A75398F4-B97A-45C2-8F3D-26CB74E37A1CQ30408732-48AE1BF4-4781-4496-9422-B8ADEAB7522BQ33411160-A5BDE5DA-DB49-440F-8792-CC4F2231E363Q35004861-5E819B2E-C8FD-4E0F-A883-79DA7BE9126CQ37406805-97E16CEA-5714-4349-BDC2-A20BA0B25767
P2860
NMR evidence for forming highly populated helical conformations in the partially folded hNck2 SH3 domain.
description
2008 nî lūn-bûn
@nan
2008 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հուլիսին 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
NMR evidence for forming highl ...... ially folded hNck2 SH3 domain.
@ast
NMR evidence for forming highl ...... ially folded hNck2 SH3 domain.
@en
type
label
NMR evidence for forming highl ...... ially folded hNck2 SH3 domain.
@ast
NMR evidence for forming highl ...... ially folded hNck2 SH3 domain.
@en
prefLabel
NMR evidence for forming highl ...... ially folded hNck2 SH3 domain.
@ast
NMR evidence for forming highl ...... ially folded hNck2 SH3 domain.
@en
P2860
P1433
P1476
NMR evidence for forming highl ...... ially folded hNck2 SH3 domain.
@en
P2093
Jingxian Liu
P2860
P304
P356
10.1529/BIOPHYSJ.107.125641
P407
P577
2008-07-03T00:00:00Z