Measurement of bond vector orientations in invisible excited states of proteins. - Wikidata - wikimedia - TriplyDB

Measurement of bond vector orientations in invisible excited states of proteins.

Measurement of bond vector orientations in invisible excited states of proteins.

http://www.wikidata.org/entity/Q36276828

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Revealing the properties of plant defensins through dynamics Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy A transient and low-populated protein-folding intermediate at atomic resolution Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study Solution structure of a minor and transiently formed state of a T4 lysozyme mutant Solution structure of the major factor VIII binding region on von Willebrand factor Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone Cold denaturation of a protein dimer monitored at atomic resolution Studying Dynamics by Magic-Angle Spinning Solid-State NMR Spectroscopy: Principles and Applications to Biomolecules The role of dynamic conformational ensembles in biomolecular recognition Determination of pseudocontact shifts of low-populated excited states by NMR chemical exchange saturation transfer.Fractional enrichment of proteins using [2-(13)C]-glycerol as the carbon source facilitates measurement of excited state 13Cα chemical shifts with improved sensitivity.Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.Measuring hydrogen exchange rates in invisible protein excited states pH-dependent transient conformational states control optical properties in cyan fluorescent protein Structural biology by NMR: structure, dynamics, and interactions.The quiet renaissance of protein nuclear magnetic resonance.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 Folding of the four-helix bundle FF domain from a compact on-pathway intermediate state is governed predominantly by water motion.Visualizing lowly-populated regions of the free energy landscape of macromolecular complexes by paramagnetic relaxation enhancement Chemical exchange in biomacromolecules: past, present, and future.Nuclear magnetic resonance captures the elusive.Visualizing transient dark states by NMR spectroscopy.Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation.The binding mechanisms of intrinsically disordered proteins.Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways.Paramagnetic-based NMR restraints lift residual dipolar coupling degeneracy in multidomain detergent-solubilized membrane proteins.Exposing the Moving Parts of Proteins with NMR Spectroscopy.Transiently populated intermediate functions as a branching point of the FF domain folding pathway Hsp70 biases the folding pathways of client proteins.NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.Probing the free energy landscapes of ALS disease mutants of SOD1 by NMR spectroscopy NMR spectroscopy brings invisible protein states into focus.Protein folding on the ribosome studied using NMR spectroscopy.NMR reveals novel mechanisms of protein activity regulation.Characterizing excited conformational states of RNA by NMR spectroscopy Measurement of protein backbone 13CO and 15N relaxation dispersion at high resolution.The linker between the dimerization and catalytic domains of the CheA histidine kinase propagates changes in structure and dynamics that are important for enzymatic activity Protein dynamics and function from solution state NMR spectroscopy.Off-resonance rotating-frame relaxation dispersion experiment for 13C in aromatic side chains using L-optimized TROSY-selection.

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P2860

Measurement of bond vector orientations in invisible excited states of proteins.

http://www.wikidata.org/entity/Q36276828

description

2007 nî lūn-bûn

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2007年の論文

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年學術文章

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2007年學術文章

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2007年學術文章

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name

Measurement of bond vector orientations in invisible excited states of proteins.

@ast

Measurement of bond vector orientations in invisible excited states of proteins.

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type

label

Measurement of bond vector orientations in invisible excited states of proteins.

@ast

Measurement of bond vector orientations in invisible excited states of proteins.

@en

prefLabel

Measurement of bond vector orientations in invisible excited states of proteins.

@ast

Measurement of bond vector orientations in invisible excited states of proteins.

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

P1476

Measurement of bond vector orientations in invisible excited states of proteins.

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P2093

D Flemming Hansen

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

Elliott Stollar

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

Eva Meirovitch

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

Pramodh Vallurupalli

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Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

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The biologically relevant targets and binding affinity requirements for the function of the yeast actin-binding protein 1 Src-homology 3 domain vary with genetic context

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

Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution.

Measurement of Proton, Nitrogen, and Carbonyl Chemical Shielding Anisotropies in a Protein Dissolved in a Dilute Liquid Crystalline Phase

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