Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution. - Wikidata - awgldk - TriplyDB

Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution.

Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution.

http://www.wikidata.org/entity/Q36472769

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Fundamental challenges in mechanistic enzymology: progress toward understanding the rate enhancements of enzymes The ensemble nature of allostery Structural Rigidity of a Large Cavity-containing Protein Revealed by High-pressure Crystallography Dynamically Coupled Residues within the SH2 Domain of FYN Are Key to Unlocking Its Activity Ezrin induces long-range interdomain allostery in the scaffolding protein NHERF1 At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis?Long-range intra-protein communication can be transmitted by correlated side-chain fluctuations alone Structure and dynamics of the G121V dihydrofolate reductase mutant: lessons from a transition-state inhibitor complex Quantitative comparison of errors in 15N transverse relaxation rates measured using various CPMG phasing schemes Perspective: Defining and quantifying the role of dynamics in enzyme catalysis Hydrophobic core mutations in CI2 globally perturb fast side-chain dynamics similarly without regard to position.Protein dynamics studied with ultrafast two-dimensional infrared vibrational echo spectroscopy.Conformational dynamics and thermodynamics of protein-ligand binding studied by NMR relaxation.Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered.Is buffer a good proxy for a crowded cell-like environment? A comparative NMR study of calmodulin side-chain dynamics in buffer and E. coli lysate Probing micro-solvation in "numbers": the case of neutral dipeptides in water.Reverse micelles as a tool for probing solvent modulation of protein dynamics: Reverse micelle encapsulated hemoglobin.Banding of NMR-derived methyl order parameters: implications for protein dynamics.Insight into the allosteric mechanism of Scapharca dimeric hemoglobin On the ability of molecular dynamics force fields to recapitulate NMR derived protein side chain order parameters.Accurate determination of rates from non-uniformly sampled relaxation data.Flexibility and Solvation of Amyloid-β Hydrophobic Core Fast Motions of Key Methyl Groups in Amyloid-β Fibrils.Protein side-chain dynamics and residual conformational entropy The physical basis of model-free analysis of NMR relaxation data from proteins and complex fluids.Contrasting roles of dynamics in protein allostery: NMR and structural studies of CheY and the third PDZ domain from PSD-95.A surprising role for conformational entropy in protein function.Extensive conformational heterogeneity within protein cores.relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and μs motion of proteins.An improved picture of methyl dynamics in proteins from slowly relaxing local structure analysis of 2H spin relaxation.Structural dynamics of bio-macromolecules by NMR: the slowly relaxing local structure approach Conformational entropy in molecular recognition by proteins.¹³C relaxation experiments for aromatic side chains employing longitudinal- and transverse-relaxation optimized NMR spectroscopy Visualizing transient dark states by NMR spectroscopy.The role of conformational entropy in molecular recognition by calmodulin.An introduction to NMR-based approaches for measuring protein dynamics.Backbone dynamics of deoxy and carbonmonoxy hemoglobin by NMR/SRLS.On the characterization of protein native state ensembles.The p66 immature precursor of HIV-1 reverse transcriptase.Temperature dependence of fast dynamics in proteins.

P2860

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P2860

Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution.

http://www.wikidata.org/entity/Q36472769

description

2006 nî lūn-bûn

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2006年の論文

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年學術文章

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2006年學術文章

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2006年學術文章

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name

Characterization of the fast d ...... ng NMR relaxation in solution.

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Characterization of the fast d ...... ng NMR relaxation in solution.

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Characterization of the fast d ...... ng NMR relaxation in solution.

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Characterization of the fast d ...... ng NMR relaxation in solution.

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Characterization of the fast d ...... ng NMR relaxation in solution.

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Characterization of the fast d ...... ng NMR relaxation in solution.

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Chemical Reviews

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Characterization of the fast d ...... ng NMR relaxation in solution.

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A Joshua Wand

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Kendra King Frederick

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Tatyana I Igumenova

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P2860

Ligand-dependent dynamics and intramolecular signaling in a PDZ domain

Side-chain dynamics of the SAP SH2 domain correlate with a binding hot spot and a region with conformational plasticity

Correlation between dynamics and high affinity binding in an SH2 domain interaction

NMR dynamics-derived insights into the binding properties of a peptide interacting with an SH2 domain

Solution structure and dynamics of a designed hydrophobic core variant of ubiquitin

MOLMOL: a program for display and analysis of macromolecular structures

Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis

The origin of protein sidechain order parameter distributions

Hydrogen exchange and structural dynamics of proteins and nucleic acids

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scholarly article

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10.1021/CR040422H

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5

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