A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.
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Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and DynamicsAutomated identification of functional dynamic contact networks from X-ray crystallographyCrystal Cryocooling Distorts Conformational Heterogeneity in a Model Michaelis Complex of DHFRThe RING 2.0 web server for high quality residue interaction networksEffects of Non-Natural Amino Acid Incorporation into the Enzyme Core Region on Enzyme Structure and Function.The Patterns of Coevolution in Clade B HIV Envelope's N-Glycosylation SitesTerahertz optical measurements of correlated motions with possible allosteric function.Computational approaches to mapping allosteric pathways.Chemical exchange in biomacromolecules: past, present, and future.A coarse-grained elastic network atom contact model and its use in the simulation of protein dynamics and the prediction of the effect of mutationsComparative laboratory evolution of ordered and disordered enzymes.Cofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway.Weighted Implementation of Suboptimal Paths (WISP): An Optimized Algorithm and Tool for Dynamical Network Analysis.Hydride Transfer in DHFR by Transition Path Sampling, Kinetic Isotope Effects, and Heavy Enzyme StudiesSide chain conformational averaging in human dihydrofolate reductase.Protein mass-modulated effects in the catalytic mechanism of dihydrofolate reductase: beyond promoting vibrations.Network of remote and local protein dynamics in dihydrofolate reductase catalysisENCoM server: exploring protein conformational space and the effect of mutations on protein function and stability.Examinations of the Chemical Step in Enzyme Catalysis.The role of protein dynamics in allosteric effects-introduction.Collision-free poisson motion planning in ultra high-dimensional molecular conformation spaces.Contribution of Buried Distal Amino Acid Residues in Horse Liver Alcohol Dehydrogenase to Structure and Catalysis.Engineered control of enzyme structural dynamics and function.Applications of Normal Mode Analysis Methods in Computational Protein Design.Protein motions and dynamic effects in enzyme catalysis.Amino-Acid Network Clique Analysis of Protein Mutation Non-Additive Effects: A Case Study of Lysozme.The Binding Mechanism Between Inositol Phosphate (InsP) and the Jasmonate Receptor Complex: A Computational Study
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P2860
A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 24 June 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.
@en
A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.
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type
label
A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.
@en
A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.
@nl
prefLabel
A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.
@en
A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.
@nl
P2093
P2860
P50
P356
P1433
P1476
A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.
@en
P2093
Dan McElheny
David D Boehr
Jason R Schnell
Stephen J Benkovic
Sung-Hun Bae
P2860
P304
P356
10.1021/BI400563C
P407
P577
2013-06-24T00:00:00Z