about
A test case for structure-based functional assignment: The 1.2 Å crystal structure of the yjgF gene product from Escherichia coliThe structure of theyrdCgene product fromEscherichia colireveals a new fold and suggests a role in RNA bindingCrystal structure of conserved hypothetical protein Aq1575 from Aquifex aeolicus.Salt Bridges Regulate Both Dimer Formation and Monomeric Flexibility in HdeB and May Have a Role in Periplasmic Chaperone FunctionProtein structure prediction by global optimization of a potential energy function.Structural similarity to link sequence space: new potential superfamilies and implications for structural genomics.Water in protein structure predictionMimicking titration experiments with MD simulations: A protocol for the investigation of pH-dependent effects on proteinsConditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.Multiscale modeling of a conditionally disordered pH-sensing chaperone.The first crystal structure of an archaeal helical repeat protein.HdeB chaperone activity is coupled to its intrinsic dynamic properties.Role of the multidrug resistance regulator MarA in global regulation of the hdeAB acid resistance operon in Escherichia coli.Coupled folding and binding with 2D Window-Exchange Umbrella Sampling.Chaperone activation by unfolding.How bacteria survive an acid trip.Comparative proteomics reveal distinct chaperone-client interactions in supporting bacterial acid resistanceProbing pH-dependent dissociation of HdeA dimers.Annotation in three dimensions. PINTS: Patterns in Non-homologous Tertiary Structures.Binding and folding of the small bacterial chaperone HdeA.Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.The Mechanism of HdeA Unfolding and Chaperone Activation.Quantitative and Comparative Profiling of Protease Substrates through a Genetically Encoded Multifunctional Photocrosslinker.Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation.Roles of structural plasticity in chaperone HdeA activity are revealed by 19F NMR.
P2860
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P2860
description
1998 nî lūn-bûn
@nan
1998 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Crystal structure of Escherichia coli HdeA
@ast
Crystal structure of Escherichia coli HdeA
@en
Crystal structure of Escherichia coli HdeA
@nl
type
label
Crystal structure of Escherichia coli HdeA
@ast
Crystal structure of Escherichia coli HdeA
@en
Crystal structure of Escherichia coli HdeA
@nl
prefLabel
Crystal structure of Escherichia coli HdeA
@ast
Crystal structure of Escherichia coli HdeA
@en
Crystal structure of Escherichia coli HdeA
@nl
P2093
P2860
P356
P1476
Crystal structure of Escherichia coli HdeA
@en
P2093
P2860
P356
10.1038/1796
P577
1998-09-01T00:00:00Z