Allostery in protein domains reflects a balance of steric and hydrophobic effects.
about
Structural and energetic basis of allosteryThe ensemble nature of allosteryOrchestration of secretory protein folding by ER chaperonesAllosteric Inhibition of a Zinc-Sensing Transcriptional Repressor: Insights into the Arsenic Repressor (ArsR) FamilyNonlinear backbone torsional pair correlations in proteinsQuantitative theory of hydrophobic effect as a driving force of protein structureStructural Basis for Modulation of Quality Control Fate in a Marginally Stable Protein.Investigating Dynamic Interdomain Allostery in Pin1Long-Range Epistasis Mediated by Structural Change in a Model of Ligand Binding ProteinsMassively parallel sampling of lattice proteins reveals foundations of thermal adaptation.RecA-mediated sequence homology recognition as an example of how searching speed in self-assembly systems can be optimized by balancing entropic and enthalpic barriers.Information-theoretic analysis and prediction of protein atomic burials: on the search for an informational intermediate between sequence and structure.Information and redundancy in the burial folding code of globular proteins within a wide range of shapes and sizes.Predicting long term cooperativity and specific modulators of receptor interactions in human transferrin from dynamics within a single microstate.
P2860
Q26825355-21135417-62B6-41EB-AE81-4D86D9F936BAQ26862004-01BD627B-50D1-49CC-8D4E-97EBA50304DBQ27013551-1D02285F-C422-45B4-B0BB-05C6F0141D1BQ27676010-84C8618D-46E9-41D5-AC28-A75FEF9A6ED3Q28391007-A2E63BC7-733F-4262-9C30-7AED43885E05Q30357723-5103B076-E835-4004-97BC-215572B7F7A7Q35875159-817D79FA-1C40-4ACC-A86A-3513A4106A3FQ36175815-748271C4-D3DA-4D37-A09D-D17A04076EFDQ36199905-DADF5AC4-E8A6-4C88-AB3A-7762F90994BAQ40645832-4C37B90B-D4FD-4B6F-A3FD-3DE26793CEF8Q41876031-84628175-D2DB-4552-AA5C-7EDD81AAE112Q47963886-E82B7FB6-8D25-4320-875B-C08539EAB1CBQ50726214-B989AE5E-BC4C-4F69-9807-AFA98A39F65FQ51459096-75B5109C-7B35-4EAB-AA01-1B3410211DEC
P2860
Allostery in protein domains reflects a balance of steric and hydrophobic effects.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
name
Allostery in protein domains reflects a balance of steric and hydrophobic effects.
@ast
Allostery in protein domains reflects a balance of steric and hydrophobic effects.
@en
type
label
Allostery in protein domains reflects a balance of steric and hydrophobic effects.
@ast
Allostery in protein domains reflects a balance of steric and hydrophobic effects.
@en
prefLabel
Allostery in protein domains reflects a balance of steric and hydrophobic effects.
@ast
Allostery in protein domains reflects a balance of steric and hydrophobic effects.
@en
P1433
P1476
Allostery in protein domains reflects a balance of steric and hydrophobic effects.
@en
P2093
Jeremy L England
P304
P356
10.1016/J.STR.2011.04.009
P577
2011-07-01T00:00:00Z