Protein dynamics investigated by inherent structure analysis.
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Crystallographic and Nuclear Magnetic Resonance Evaluation of the Impact of Peptide Binding to the Second PDZ Domain of Protein Tyrosine Phosphatase 1ERigid Residue Scan Simulations Systematically Reveal Residue Entropic Roles in Protein AllosteryBeyond the binding site: the role of the β₂-β₃ loop and extra-domain structures in PDZ domainsA comparative analysis of clustering algorithms: O2 migration in truncated hemoglobin I from transition networks.Mapping the intrinsically disordered properties of the flexible loop domain of Bcl-2: a molecular dynamics simulation study.Inherent structure versus geometric metric for state space discretization.Coupling Protein Dynamics with Proton Transport in Human Carbonic Anhydrase II.Elucidating the role of disulfide bond on amyloid formation and fibril reversibility of somatostatin-14: relevance to its storage and secretionPerspectives on: ion selectivity: design principles for K+ selectivity in membrane transport.Systematically constructing kinetic transition network in polypeptide from top to down: trajectory mapping.Hidden protein folding pathways in free-energy landscapes uncovered by network analysis.The Two Dimensional Vibrational Echo of a Nitrile Probe of the Villin HP35 Protein.Beyond microscopic reversibility: Are observable non-equilibrium processes precisely reversible?Network visualization of conformational sampling during molecular dynamics simulation.A kinetic approach to the sequence-aggregation relationship in disease-related protein assemblyCluster analysis of molecular simulation trajectories for systems where both conformation and orientation of the sampled states are importantConsensus for the Fip35 folding mechanism?Quantum clustering and network analysis of MD simulation trajectories to probe the conformational ensembles of protein-ligand interactions.Implications of short time scale dynamics on long time processes.Coexisting origins of subdiffusion in internal dynamics of proteins.Accounting for the kinetics in order parameter analysis: lessons from theoretical models and a disordered peptide.Thermodynamics and kinetics of large-time-step molecular dynamics.Protein inherent structures by different minimization strategies.
P2860
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P2860
Protein dynamics investigated by inherent structure analysis.
description
2010 nî lūn-bûn
@nan
2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2010年の論文
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2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
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2010年學術文章
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name
Protein dynamics investigated by inherent structure analysis.
@ast
Protein dynamics investigated by inherent structure analysis.
@en
type
label
Protein dynamics investigated by inherent structure analysis.
@ast
Protein dynamics investigated by inherent structure analysis.
@en
prefLabel
Protein dynamics investigated by inherent structure analysis.
@ast
Protein dynamics investigated by inherent structure analysis.
@en
P2860
P356
P1476
Protein dynamics investigated by inherent structure analysis.
@en
P2093
Francesco Rao
P2860
P304
P356
10.1073/PNAS.0915087107
P407
P577
2010-04-30T00:00:00Z