Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry - Test2 - elhamkhani - TriplyDB

Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry

Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry

http://www.wikidata.org/entity/Q28661085

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Detection of correlated conformational fluctuations in intrinsically disordered proteins through paramagnetic relaxation interference.Adaptive resolution simulation of a biomolecule and its hydration shell: Structural and dynamical properties.The "long tail" of the protein tumbling correlation function: observation by (1)H NMR relaxometry in a wide frequency and concentration range.Sample Shuttling Relaxometry of Contrast Agents: NMRD Profiles above 1 T with a Single Device Distribution of Pico- and Nanosecond Motions in Disordered Proteins from Nuclear Spin Relaxation Dynamic Nuclear Polarization Fast Field Cycling Method for the Selective Study of Molecular Dynamics in Block Copolymers.Protein dynamics from nuclear magnetic relaxation.Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR.Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements.Ultra-wide range field-dependent measurements of the relaxivity of Gd1-xEuxVO4 nanoparticle contrast agents using a mechanical sample-shuttling relaxometer.Simple method for the generation of multiple homogeneous field volumes inside the bore of superconducting magnets.Substrate and Cofactor Dynamics on Guanosine Monophosphate Reductase Probed by High Resolution Field Cycling 31P NMR Relaxometry.Determination of Protein ps-ns Motions by High-Resolution Relaxometry.Anion induced conformational preference of Cα NN motif residues in functional proteins.Recovering Invisible Signals by Two-Field NMR Spectroscopy.Full Correlations across Broad NMR Spectra by Two-Field Total Correlation Spectroscopy.High-resolution two-field nuclear magnetic resonance spectroscopy.Partial-Homogeneity-Based Two-Dimensional High-Resolution Nuclear Magnetic Resonance Spectroscopy under Inhomogeneous Magnetic Fields.High sensitivity high-resolution full range relaxometry using a fast mechanical sample shuttling device and a cryo-probe.High resolution NMR study of T₁ magnetic relaxation dispersion. IV. Proton relaxation in amino acids and Met-enkephalin pentapeptide.

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P2860

Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry

http://www.wikidata.org/entity/Q28661085

description

2013 nî lūn-bûn

@nan

2013 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry

@ast

Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry

@en

Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry

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type

label

Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry

@ast

Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry

@en

Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry

@nl

prefLabel

Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry

@ast

Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry

@en

Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry

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Journal of the American Chemical Society

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Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry

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P2093

Fabien Ferrage

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Frank Engelke

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Geoffrey Bodenhausen

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Philippe Pelupessy

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Shahid Nawaz Khan

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Thorsten Marquardsen

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

Volker Reiss

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P2860

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

Solution Structure of the NaV1.2 C-terminal EF-hand Domain

Weak Long-Range Correlated Motions in a Surface Patch of Ubiquitin Involved in Molecular Recognition

Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Ubiquitin-binding domains - from structures to functions

A hierarchy of timescales in protein dynamics is linked to enzyme catalysis

Microsecond molecular dynamics simulation shows effect of slow loop dynamics on backbone amide order parameters of proteins

Self-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics.

Toward a unified representation of protein structural dynamics in solution.

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18665-18672

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scholarly article

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10.1021/JA409820G

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49

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135

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Dimitrios Sakellariou

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2013-11-26T00:00:00Z

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