On the roles of substrate binding and hinge unfolding in conformational changes of adenylate kinase.
about
Allosteric activation transitions in enzymes and biomolecular motors: insights from atomistic and coarse-grained simulationsExploring the conformational transitions of biomolecular systems using a simple two-state anisotropic network model"Fluctuograms" reveal the intermittent intra-protein communication in subtilisin Carlsberg and correlate mechanical coupling with co-evolutionAllostery in the ferredoxin protein motif does not involve a conformational switchInterconversion of functional motions between mesophilic and thermophilic adenylate kinasesEvent detection and sub-state discovery from biomolecular simulations using higher-order statistics: application to enzyme adenylate kinase.WEBnm@ v2.0: Web server and services for comparing protein flexibilityConformational dynamics of a ligand-free adenylate kinase.Enzyme closure and nucleotide binding structurally lock guanylate kinase.Structural distributions from single-molecule measurements as a tool for molecular mechanics.Large-scale motions in the adenylate kinase solution ensemble: coarse-grained simulations and comparison with solution X-ray scattering.Active-Loop Dynamics within the Michaelis Complex of Lactate Dehydrogenase from Bacillus stearothermophilus.Mapping the Dynamics Landscape of Conformational Transitions in Enzyme: The Adenylate Kinase Case.Transitions to catalytically inactive conformations in EGFR kinaseBiomolecular dynamics: order-disorder transitions and energy landscapesStructural basis for catalytically restrictive dynamics of a high-energy enzyme state.Global transitions of proteins explored by a multiscale hybrid methodology: application to adenylate kinase.Molecular dynamics studies on the conformational transitions of adenylate kinase: a computational evidence for the conformational selection mechanism.Substrate Binding Specifically Modulates Domain Arrangements in Adenylate Kinase.Structural basis for ligand binding to an enzyme by a conformational selection pathway.Opening mechanism of adenylate kinase can vary according to selected molecular dynamics force field.Sampling large conformational transitions: adenylate kinase as a testing ground
P2860
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P2860
On the roles of substrate binding and hinge unfolding in conformational changes of adenylate kinase.
description
2010 nî lūn-bûn
@nan
2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
On the roles of substrate bind ...... l changes of adenylate kinase.
@ast
On the roles of substrate bind ...... l changes of adenylate kinase.
@en
On the roles of substrate bind ...... l changes of adenylate kinase.
@nl
type
label
On the roles of substrate bind ...... l changes of adenylate kinase.
@ast
On the roles of substrate bind ...... l changes of adenylate kinase.
@en
On the roles of substrate bind ...... l changes of adenylate kinase.
@nl
prefLabel
On the roles of substrate bind ...... l changes of adenylate kinase.
@ast
On the roles of substrate bind ...... l changes of adenylate kinase.
@en
On the roles of substrate bind ...... l changes of adenylate kinase.
@nl
P2860
P1433
P1476
On the roles of substrate bind ...... al changes of adenylate kinase
@en
P2093
Jason B Brokaw
P2860
P304
P356
10.1016/J.BPJ.2010.09.040
P407
P50
P577
2010-11-01T00:00:00Z