Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings. - Wikidata - awgldk - TriplyDB

Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings.

Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings.

http://www.wikidata.org/entity/Q34048098

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Enzymes: An integrated view of structure, dynamics and function NMR Methods to Study Dynamic Allostery Modeling conformational ensembles of slow functional motions in Pin1-WW Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution Hydrogen Bond Coupling in the Ketosteroid Isomerase Active Site A Correspondence Between Solution-State Dynamics of an Individual Protein and the Sequence and Conformational Diversity of its Family Pressure-Dependent Structure Changes in Barnase on Ligand Binding Reveal Intermediate Rate Fluctuations Weak Long-Range Correlated Motions in a Surface Patch of Ubiquitin Involved in Molecular Recognition Integrated description of protein dynamics from room-temperature X-ray crystallography and NMR Improved Cross Validation of a Static Ubiquitin Structure Derived from High Precision Residual Dipolar Couplings Measured in a Drug-Based Liquid Crystalline Phase Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs Integrative, dynamic structural biology at atomic resolution--it's about time Nonlinear backbone torsional pair correlations in proteins Long-range intra-protein communication can be transmitted by correlated side-chain fluctuations alone VPS29 is not an active metallo-phosphatase but is a rigid scaffold required for retromer interaction with accessory proteins Correlated inter-domain motions in adenylate kinase Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry Multi-timescale conformational dynamics of the SH3 domain of CD2-associated protein using NMR spectroscopy and accelerated molecular dynamics Dynamics may significantly influence the estimation of interatomic distances in biomolecular X-ray structures Protein structure validation and identification from unassigned residual dipolar coupling data using 2D-PDPA.Molecular crowding inhibits intramolecular breathing motions in proteins.Self-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics.Structural biology by NMR: structure, dynamics, and interactions.16-fold degeneracy of peptide plane orientations from residual dipolar couplings: analytical treatment and implications for protein structure determination Toward a unified representation of protein structural dynamics in solution.Simultaneous structure and dynamics of a membrane protein using REDCRAFT: membrane-bound form of Pf1 coat protein.Conformational dynamics and thermodynamics of protein-ligand binding studied by NMR relaxation.Measuring residual dipolar couplings at high hydrostatic pressure: robustness of alignment media to high pressure.Protein dynamics. Direct observation of hierarchical protein dynamics.Solvent-induced differentiation of protein backbone hydrogen bonds in calmodulin.Scrutinizing molecular mechanics force fields on the submicrosecond timescale with NMR data.Site-specific backbone amide (15)N chemical shift anisotropy tensors in a small protein from liquid crystal and cross-correlated relaxation measurements.Efficient and accurate estimation of relative order tensors from lambda-maps Polarizable atomic multipole x-ray refinement: hydration geometry and application to macromolecules MAVENs: motion analysis and visualization of elastic networks and structural ensembles.Measurement of (1)H-(15)N and (1)H-(13)C residual dipolar couplings in nucleic acids from TROSY intensities.Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N-15N and carbonyl 13C-13C dipolar recoupling data.Nonexponential decay of internal rotational correlation functions of native proteins and self-similar structural fluctuations.A mechanistic understanding of allosteric immune escape pathways in the HIV-1 envelope glycoprotein.Advances in the REDCAT software package.

P2860

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P2860

Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings.

http://www.wikidata.org/entity/Q34048098

description

2005 nî lūn-bûn

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2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Identification of slow correla ...... ydrogen-bond scalar couplings.

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Identification of slow correla ...... ydrogen-bond scalar couplings.

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Identification of slow correla ...... ydrogen-bond scalar couplings.

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type

label

Identification of slow correla ...... ydrogen-bond scalar couplings.

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Identification of slow correla ...... ydrogen-bond scalar couplings.

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Identification of slow correla ...... ydrogen-bond scalar couplings.

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prefLabel

Identification of slow correla ...... ydrogen-bond scalar couplings.

@ast

Identification of slow correla ...... ydrogen-bond scalar couplings.

@en

Identification of slow correla ...... ydrogen-bond scalar couplings.

@nl

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PNAS.0505129102

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Identification of slow correla ...... hydrogen-bond scalar couplings

@en

P2093

Kyuil Cho

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

Martin Blackledge

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

Rafael Brüschweiler

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P2860

The third IgG-binding domain from streptococcal protein G. An analysis by X-ray crystallography of the structure alone and in a complex with Fab

Protein structure prediction and structural genomics

NMR structures of biomolecules using field oriented media and residual dipolar couplings

Protein backbone dynamics from N-HN dipolar couplings in partially aligned systems: a comparison of motional models in the presence of structural noise

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

Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions

The energy landscapes and motions of proteins

Studying excited states of proteins by NMR spectroscopy.

New approaches to the dynamic interpretation and prediction of NMR relaxation data from proteins.

A perspective on enzyme catalysis.

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13885-13890

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scholarly article

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10.1073/PNAS.0505129102

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39

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102

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Sebastian Meier

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Guillaume Bouvignies

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7592197

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16172390

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1236556

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