Toward a unified representation of protein structural dynamics in solution. - Wikidata - awgldk - TriplyDB

Toward a unified representation of protein structural dynamics in solution.

Toward a unified representation of protein structural dynamics in solution.

http://www.wikidata.org/entity/Q30382603

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Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies Dynamics, flexibility and ligand-induced conformational changes in biological macromolecules: a computational approach Relating sequence encoded information to form and function of intrinsically disordered proteins Modeling conformational ensembles of slow functional motions in Pin1-WW Weak Long-Range Correlated Motions in a Surface Patch of Ubiquitin Involved in Molecular Recognition Trapping the dynamic acyl carrier protein in fatty acid biosynthesis Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry DNA Polymerase Conformational Dynamics and the Role of Fidelity-Conferring Residues: Insights from Computational Simulations Multi-timescale conformational dynamics of the SH3 domain of CD2-associated protein using NMR spectroscopy and accelerated molecular dynamics The dynamic structure of thrombin in solution Ensemble-based interpretations of NMR structural data to describe protein internal dynamics.Advances in automated NMR protein structure determination.Disease-associated mutations disrupt functionally important regions of intrinsic protein disorder Mechanisms of intramolecular communication in a hyperthermophilic acylaminoacyl peptidase: a molecular dynamics investigation.Scrutinizing molecular mechanics force fields on the submicrosecond timescale with NMR data.In silico elucidation of the recognition dynamics of ubiquitin Accessing a hidden conformation of the maltose binding protein using accelerated molecular dynamics Protein loop closure using orientational restraints from NMR data Studying functional dynamics in bio-molecules using accelerated molecular dynamics.An introduction to NMR-based approaches for measuring protein dynamics.On the Use of Accelerated Molecular Dynamics to Enhance Configurational Sampling in Ab Initio Simulations.Hot spots in a network of functional sites.Accelerating chemical reactions: exploring reactive free-energy surfaces using accelerated ab initio molecular dynamics Implementation of Accelerated Molecular Dynamics in NAMD Intrinsic disorder in measles virus nucleocapsids.Enhanced Lipid Diffusion and Mixing in Accelerated Molecular Dynamics.Longer simulations sample larger subspaces of conformations while maintaining robust mechanisms of motion Resolving the complex role of enzyme conformational dynamics in catalytic function.Assessing and refining molecular dynamics simulations of proteins with nuclear magnetic resonance data.Modulating RNA Alignment Using Directional Dynamic Kinks: Application in Determining an Atomic-Resolution Ensemble for a Hairpin using NMR Residual Dipolar Couplings.Advances in the determination of nucleic acid conformational ensembles Allosteric switch regulates protein-protein binding through collective motion.A general method for constructing atomic-resolution RNA ensembles using NMR residual dipolar couplings: the basis for interhelical motions revealed.Mapping the structural and dynamical features of kinesin motor domains Biomolecularmodeling and simulation: a field coming of age.Characterizing weak protein-protein complexes by NMR residual dipolar couplings.Towards a robust description of intrinsic protein disorder using nuclear magnetic resonance spectroscopy.Understanding biomolecular motion, recognition, and allostery by use of conformational ensembles.Measuring dynamic and kinetic information in the previously inaccessible supra-τ(c) window of nanoseconds to microseconds by solution NMR spectroscopy.

P2860

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P2860

Toward a unified representation of protein structural dynamics in solution.

http://www.wikidata.org/entity/Q30382603

description

2009 nî lūn-bûn

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2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Toward a unified representation of protein structural dynamics in solution.

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Toward a unified representation of protein structural dynamics in solution.

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type

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Toward a unified representation of protein structural dynamics in solution.

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Toward a unified representation of protein structural dynamics in solution.

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Toward a unified representation of protein structural dynamics in solution.

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Toward a unified representation of protein structural dynamics in solution.

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Journal of the American Chemical Society

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Toward a unified representation of protein structural dynamics in solution.

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P2093

Martin Blackledge

http://www.w3.org/2001/XMLSchema#string

Phineus R L Markwick

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P2860

Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution

Structure of ubiquitin refined at 1.8 A resolution

"Ensemble" iterative relaxation matrix approach: a new NMR refinement protocol applied to the solution structure of crambin

Comparison of multiple Amber force fields and development of improved protein backbone parameters

A novel approach to the retrieval of structural and dynamic information from residual dipolar couplings using several oriented media in biomolecular NMR spectroscopy

Molecular dynamics and protein function.

Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium

NMR evidence for slow collective motions in cyanometmyoglobin

Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease

The energy landscapes and motions of proteins

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46

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131

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Guillaume Bouvignies

J. Andrew McCammon

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2009-11-01T00:00:00Z

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