Nanometer propagation of millisecond motions in V-type allostery.
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NMR Methods to Study Dynamic AllosteryNMR insights into protein allosteryExploring protein structure and dynamics through a project-oriented biochemistry laboratory module.Contrasting roles of dynamics in protein allostery: NMR and structural studies of CheY and the third PDZ domain from PSD-95.Allosteric pathways in imidazole glycerol phosphate synthase.Exploring residue component contributions to dynamical network models of allosteryMapping allostery through the covariance analysis of NMR chemical shiftsDynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy.Stereospecific gating of functional motions in Pin1Mapping the Hydrogen Bond Networks in the Catalytic Subunit of Protein Kinase A Using H/D Fractionation FactorsExposing the Moving Parts of Proteins with NMR Spectroscopy.Allosteric Communication Disrupted by a Small Molecule Binding to the Imidazole Glycerol Phosphate Synthase Protein-Protein Interface.Clusters of branched aliphatic side chains serve as cores of stability in the native state of the HisF TIM barrel protein.Solution NMR Spectroscopy for the Study of Enzyme Allostery.What Mutagenesis Can and Cannot Reveal About Allostery.Chemical shift imprint of intersubunit communication in a symmetric homodimer.Protein Allostery and Conformational Dynamics.NMR reveals a dynamic allosteric pathway in thrombin.NMR reveals novel mechanisms of protein activity regulation.Allostery and binding cooperativity of the catalytic subunit of protein kinase A by NMR spectroscopy and molecular dynamics simulations.Control limits for accumulation of plant metabolites: brute force is no substitute for understanding.Applications of NMR and computational methodologies to study protein dynamics.Identification of regions of rabbit muscle pyruvate kinase important for allosteric regulation by phenylalanine, detected by H/D exchange mass spectrometry.Monitoring allostery in D2O: a necessary control in studies using hydrogen/deuterium exchange to characterize allosteric regulation.Dynamically Driven Protein Allostery Exhibits Disparate Responses for Fast and Slow Motions.Dissecting Dynamic Allosteric Pathways Using Chemically Related Small-Molecule Activators.Altering the allosteric pathway in IGPS suppresses millisecond motions and catalytic activitySolution NMR and computational methods for understanding protein allostery.Accelerating multidimensional NMR and MRI experiments using iterated maps.Synchronous opening and closing motions are essential for cAMP-dependent protein kinase A signaling.Engineered control of enzyme structural dynamics and function.Glutamine Hydrolysis by Imidazole Glycerol Phosphate Synthase Displays Temperature Dependent Allosteric Activation.
P2860
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P2860
Nanometer propagation of millisecond motions in V-type allostery.
description
2010 nî lūn-bûn
@nan
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
2010年论文
@zh
2010年论文
@zh-cn
name
Nanometer propagation of millisecond motions in V-type allostery.
@en
type
label
Nanometer propagation of millisecond motions in V-type allostery.
@en
prefLabel
Nanometer propagation of millisecond motions in V-type allostery.
@en
P2860
P1433
P1476
Nanometer propagation of millisecond motions in V-type allostery.
@en
P2093
J Patrick Loria
James M Lipchock
P2860
P304
P356
10.1016/J.STR.2010.09.020
P577
2010-12-01T00:00:00Z