Multifrequency electron spin resonance study of the dynamics of spin labeled T4 lysozyme. - Wikidata - wikimedia - TriplyDB

Multifrequency electron spin resonance study of the dynamics of spin labeled T4 lysozyme.

Multifrequency electron spin resonance study of the dynamics of spin labeled T4 lysozyme.

http://www.wikidata.org/entity/Q33832314

about

Use of electron paramagnetic resonance to solve biochemical problems Mapping molecular flexibility of proteins with site-directed spin labeling: a case study of myoglobin.Structure and dynamics of an imidazoline nitroxide side chain with strongly hindered internal motion in proteins.Structural dynamics of bio-macromolecules by NMR: the slowly relaxing local structure approach A rigid disulfide-linked nitroxide side chain simplifies the quantitative analysis of PRE data.Monomeric and dimeric conformation of the vinculin tail five-helix bundle in solution studied by EPR spectroscopy.Tau binds to lipid membrane surfaces via short amphipathic helices located in its microtubule-binding repeats Conformational distributions at the N-peptide/boxB RNA interface studied using site-directed spin labeling.High-pressure EPR reveals conformational equilibria and volumetric properties of spin-labeled proteins.A nucleotide-independent nitroxide probe reports on site-specific stereomeric environment in DNA Phase cycling with a 240 GHz, free electron laser-powered electron paramagnetic resonance spectrometer.EPR assessment of protein sites for incorporation of Gd(III) MRI contrast labels Channel and nonchannel forms of spin-labeled gramicidin in membranes and their equilibria.Continuous wave W- and D-band EPR spectroscopy offer "sweet-spots" for characterizing conformational changes and dynamics in intrinsically disordered proteins.Spin-label saturation-recovery EPR at W-band: applications to eye lens lipid membranes Structure and dynamics of a conformationally constrained nitroxide side chain and applications in EPR spectroscopy.Structure-relaxation mechanism for the response of T4 lysozyme cavity mutants to hydrostatic pressure Focus: Two-dimensional electron-electron double resonance and molecular motions: The challenge of higher frequencies Conformational distributions and hydrogen bonding in gel and frozen lipid bilayers: a high frequency spin-label ESR study.The world as viewed by and with unpaired electrons Dynamics and ordering of lipid spin-labels along the coexistence curve of two membrane phases: an ESR study.Using spin-label W-band EPR to study membrane fluidity profiles in samples of small volume.Spin labeling and Double Electron-Electron Resonance (DEER) to Deconstruct Conformational Ensembles of HIV Protease.Nonlinear scaling of surface water diffusion with bulk water viscosity of crowded solutions.Circular dichroism and site-directed spin labeling reveal structural and dynamical features of high-pressure states of myoglobin.Technological advances in site-directed spin labeling of proteins.Parameter Estimation as a Problem in Statistical Thermodynamics.EPR Studies of Gating Mechanisms in Ion Channels.Local Ordering at Mobile Sites in Proteins from Nuclear Magnetic Resonance Relaxation: The Role of Site Symmetry.Protein Dynamics in the Solid State from (2)H NMR Line Shape Analysis. II. MOMD Applied to C-D and C-CD3 Probes.Molecular crowding impacts the structure of apolipoprotein A-I with potential implications on in vivo metabolism and function.Analysis of the solution conformations of T4 lysozyme by paramagnetic NMR spectroscopy.Effect of freezing conditions on distances and their distributions derived from Double Electron Electron Resonance (DEER): a study of doubly-spin-labeled T4 lysozyme.The internal dynamics of mini c TAR DNA probed by electron paramagnetic resonance of nitroxide spin-labels at the lower stem, the loop, and the bulge.A single-stranded junction modulates nanosecond motional ordering of the substrate recognition duplex of a group I ribozyme.1H NMR relaxation in glycerol solutions of nitroxide radicals: effects of translational and rotational dynamics.Spin Probe Multi-Frequency EPR Study of Unprocessed Cotton Fibers.1H relaxation dispersion in solutions of nitroxide radicals: effects of hyperfine interactions with 14N and 15N nuclei.Orientation order and rotation mobility of nitroxide biradicals determined by quantitative simulation of EPR spectra.A New Wavelet Denoising Method for Selecting Decomposition Levels and Noise Thresholds.

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P2860

Multifrequency electron spin resonance study of the dynamics of spin labeled T4 lysozyme.

http://www.wikidata.org/entity/Q33832314

description

2010 nî lūn-bûn

@nan

2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

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2010年論文

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2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

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2010年论文

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name

Multifrequency electron spin resonance study of the dynamics of spin labeled T4 lysozyme.

@ast

Multifrequency electron spin resonance study of the dynamics of spin labeled T4 lysozyme.

@en

type

label

Multifrequency electron spin resonance study of the dynamics of spin labeled T4 lysozyme.

@ast

Multifrequency electron spin resonance study of the dynamics of spin labeled T4 lysozyme.

@en

prefLabel

Multifrequency electron spin resonance study of the dynamics of spin labeled T4 lysozyme.

@ast

Multifrequency electron spin resonance study of the dynamics of spin labeled T4 lysozyme.

@en

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Journal of Physical Chemistry B

P1476

Multifrequency electron spin resonance study of the dynamics of spin labeled T4 lysozyme.

@en

P2093

Dmitriy S Tipikin

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

Jack H Freed

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

Jozef K Moscicki

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

Keith A Earle

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

Mark R Fleissner

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Zhichun Liang

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

Ziwei Zhang

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

P2860

Exploring subdomain cooperativity in T4 lysozyme I: Structural and energetic studies of a circular permutant and protein fragment

Structural determinants of nitroxide motion in spin-labeled proteins: Solvent-exposed sites in helix B of T4 lysozyme

Structural origin of weakly ordered nitroxide motion in spin-labeled proteins

A mutant T4 lysozyme displays five different crystal conformations

Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution

Recent advances and applications of site-directed spin labeling.

Analysis of nitroxide spin label motion in a protein-protein complex using multiple frequency EPR spectroscopy.

Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics.

Microscopic viscosity and rotational diffusion of proteins in a macromolecular environment

Identifying conformational changes with site-directed spin labeling.

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5503-5521

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scholarly article

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10.1021/JP910606H

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16

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114

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Wayne L. Hubbell

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2010-04-01T00:00:00Z

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42973671

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20361789

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2865245

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