NMR mapping of protein conformational landscapes using coordinated behavior of chemical shifts upon ligand binding.
about
Biophysical and computational methods to analyze amino acid interaction networks in proteinsNMR Characterization of Information Flow and Allosteric Communities in the MAP Kinase p38γSevering of a hydrogen bond disrupts amino acid networks in the catalytically active state of the alpha subunit of tryptophan synthase.Structure-based network analysis of activation mechanisms in the ErbB family of receptor tyrosine kinases: the regulatory spine residues are global mediators of structural stability and allosteric interactions.Tracking Equilibrium and Nonequilibrium Shifts in Data with TREND.Dysfunctional conformational dynamics of protein kinase A induced by a lethal mutant of phospholamban hinder phosphorylation.Network of long-range concerted chemical shift displacements upon ligand binding to human angiogenin.Lipid binding protein response to a bile acid library: a combined NMR and statistical approach.Mapping the Hydrogen Bond Networks in the Catalytic Subunit of Protein Kinase A Using H/D Fractionation FactorsCracking the allosteric code of NMR chemical shiftsOncogenic Mutations Differentially Affect Bax Monomer, Dimer, and Oligomeric Pore Formation in the Membrane.Uncoupling Catalytic and Binding Functions in the Cyclic AMP-Dependent Protein Kinase AApplications of NMR and computational methodologies to study protein dynamics.Multiple Ligand-Bound States of a Phosphohexomutase Revealed by Principal Component Analysis of NMR Peak Shifts.A tool set to map allosteric networks through the NMR chemical shift covariance analysis.Free energy landscape remodeling of the cardiac pacemaker channel explains the molecular basis of familial sinus bradycardiaA dynamic hydrophobic core orchestrates allostery in protein kinases.Synchronous opening and closing motions are essential for cAMP-dependent protein kinase A signaling.Implementation of the NMR CHEmical Shift Covariance Analysis (CHESCA): A Chemical Biologist's Approach to Allostery.Binding mechanism and dynamic conformational change of C subunit of PKA with different pathways.Molecular Docking, Molecular Dynamics Simulations, Computational Screening to Design Quorum Sensing Inhibitors Targeting LuxP of Vibrio harveyi and Its Biological Evaluation.
P2860
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P2860
NMR mapping of protein conformational landscapes using coordinated behavior of chemical shifts upon ligand binding.
description
2014 nî lūn-bûn
@nan
2014 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի մարտին հրատարակված գիտական հոդված
@hy
2014年の論文
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2014年論文
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2014年論文
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2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
NMR mapping of protein conform ...... al shifts upon ligand binding.
@ast
NMR mapping of protein conform ...... al shifts upon ligand binding.
@en
type
label
NMR mapping of protein conform ...... al shifts upon ligand binding.
@ast
NMR mapping of protein conform ...... al shifts upon ligand binding.
@en
prefLabel
NMR mapping of protein conform ...... al shifts upon ligand binding.
@ast
NMR mapping of protein conform ...... al shifts upon ligand binding.
@en
P2093
P2860
P356
P1476
NMR mapping of protein conform ...... al shifts upon ligand binding.
@en
P2093
Gianluigi Veglia
Jonggul Kim
P2860
P304
P356
10.1039/C4CP00110A
P407
P577
2014-03-07T00:00:00Z