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Glassy dynamics of protein methyl groups revealed by deuteron NMR.

Glassy dynamics of protein methyl groups revealed by deuteron NMR.

http://www.wikidata.org/entity/Q36714440

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Peptide and Protein Dynamics and Low-Temperature/DNP Magic Angle Spinning NMR.Protein dynamics. Direct observation of hierarchical protein dynamics.Fast Motions of Key Methyl Groups in Amyloid-β Fibrils.(15)N CSA tensors and (15)N-(1)H dipolar couplings of protein hydrophobic core residues investigated by static solid-state NMR.Dynamics of Hydrophobic Core Phenylalanine Residues Probed by Solid-State Deuteron NMR.Static solid-state 2H NMR methods in studies of protein side-chain dynamics.Solid state deuterium NMR study of LKα14 peptide aggregation in biosilica.Protein dynamics in the solid state from 2H NMR line shape analysis: a consistent perspective.Restricted diffusion of methyl groups in proteins revealed by deuteron NMR: manifestation of intra-well dynamics.(1)H and (19)F spin-lattice relaxation and CH3 or CF3 reorientation in molecular solids containing both H and F atoms.Comparative Dynamics of Methionine Side-Chain in FMOC-Methionine and in Amyloid Fibrils.Distributions of methyl group rotational barriers in polycrystalline organic solids

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P2860

Glassy dynamics of protein methyl groups revealed by deuteron NMR.

http://www.wikidata.org/entity/Q36714440

description

2013 nî lūn-bûn

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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

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2013年論文

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2013年论文

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2013年论文

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2013年论文

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name

Glassy dynamics of protein methyl groups revealed by deuteron NMR.

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Glassy dynamics of protein methyl groups revealed by deuteron NMR.

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type

label

Glassy dynamics of protein methyl groups revealed by deuteron NMR.

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Glassy dynamics of protein methyl groups revealed by deuteron NMR.

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prefLabel

Glassy dynamics of protein methyl groups revealed by deuteron NMR.

@ast

Glassy dynamics of protein methyl groups revealed by deuteron NMR.

@en

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Journal of Physical Chemistry B

P1476

Glassy dynamics of protein methyl groups revealed by deuteron NMR.

@en

P2093

Dmitry Ostrovsky

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

Gina L Hoatson

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

Kirsten Penland

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

Liliya Vugmeyster

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

Robert L Vold

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

P2860

NMR structure of the 35-residue villin headpiece subdomain

The energy landscapes and motions of proteins

Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion.

Measurement of methyl group motional parameters of invisible, excited protein states by NMR spectroscopy.

Protein side-chain dynamics as observed by solution- and solid-state NMR spectroscopy: a similarity revealed.

Methyl rotation barriers in proteins from 2H relaxation data. Implications for protein structure.

Protein side-chain dynamics observed by solution- and solid-state NMR: comparative analysis of methyl 2H relaxation data.

The response of internal dynamics to hydrophobic core mutations in the SH3 domain from the Fyn tyrosine kinase

Dynamic activation of protein function: a view emerging from NMR spectroscopy.

Hydrophobic core mutations in CI2 globally perturb fast side-chain dynamics similarly without regard to position.

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1051-1061

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scholarly article

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10.1021/JP311112J

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4

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117

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2013-01-22T00:00:00Z

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23301823

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3607545

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