NMR evidence for slow collective motions in cyanometmyoglobin - Wikidata - awgldk - TriplyDB

NMR evidence for slow collective motions in cyanometmyoglobin

NMR evidence for slow collective motions in cyanometmyoglobin

http://www.wikidata.org/entity/Q28307268

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Quaternary structure built from subunits combining NMR and small-angle x-ray scattering data.NMR Methods to Study Dynamic Allostery Unveiling Inherent Degeneracies in Determining Population-Weighted Ensembles of Interdomain Orientational Distributions Using NMR Residual Dipolar Couplings: Application to RNA Helix Junction Helix Motifs.Crystal structures of myoglobin-ligand complexes at near-atomic resolution.A Correspondence Between Solution-State Dynamics of an Individual Protein and the Sequence and Conformational Diversity of its Family Pressure-Dependent Structure Changes in Barnase on Ligand Binding Reveal Intermediate Rate Fluctuations The catalytic domain of MMP-1 studied through tagged lanthanides pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods Structures of the Excited States of Phospholamban and Shifts in Their Populations upon Phosphorylation Structure and sequence elements of the CR4/5 domain of medaka telomerase RNA important for telomerase function Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings Structural determinants for ligand capture by a class II preQ 1 riboswitch Integrative, dynamic structural biology at atomic resolution--it's about time BioMagResBank Multi-timescale conformational dynamics of the SH3 domain of CD2-associated protein using NMR spectroscopy and accelerated molecular dynamics The dynamic structure of thrombin in solution Weak alignment offers new NMR opportunities to study protein structure and dynamics.Molecular crowding inhibits intramolecular breathing motions in proteins.Self-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics.Structural biology by NMR: structure, dynamics, and interactions.Toward a unified representation of protein structural dynamics in solution.Simultaneous structure and dynamics of a membrane protein using REDCRAFT: membrane-bound form of Pf1 coat protein.Residual dipolar couplings: are multiple independent alignments always possible?Aromatic Ring Currents at a Protein Surface: Use of (1)H-NMR Chemical Shifts to Refine the Structure of a Naked β Sheet.Clustering of low-energy conformations near the native structures of small proteins.Approximate reconstruction of continuous spatially complex domain motions by multialignment NMR residual dipolar couplings.PhosphoThr peptide binding globally rigidifies much of the FHA domain from Arabidopsis receptor kinase-associated protein phosphatase Structural dynamics of a single-stranded RNA-helix junction using NMR.Insights into Watson-Crick/Hoogsteen breathing dynamics and damage repair from the solution structure and dynamic ensemble of DNA duplexes containing m1A.Measurement and interpretation of 15N-1H residual dipolar couplings in larger proteins.Normal mode analysis of biomolecular structures: functional mechanisms of membrane proteins.MAVENs: motion analysis and visualization of elastic networks and structural ensembles.Protein loop closure using orientational restraints from NMR data 15N-1H Residual dipolar coupling analysis of native and alkaline-K79A Saccharomyces cerevisiae cytochrome c.Nuclear magnetic resonance of membrane-associated peptides and proteins Advances in the REDCAT software package.Dynamic motions of the HIV-1 frameshift site RNA.Mass spectrometric approaches using electrospray ionization charge states and hydrogen-deuterium exchange for determining protein structures and their conformational changes.Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation

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P2860

NMR evidence for slow collective motions in cyanometmyoglobin

http://www.wikidata.org/entity/Q28307268

description

1997 nî lūn-bûn

@nan

1997 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

1997 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

1997年の論文

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1997年論文

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1997年論文

@zh-hant

1997年論文

@zh-hk

1997年論文

@zh-mo

1997年論文

@zh-tw

1997年论文

@wuu

name

NMR evidence for slow collective motions in cyanometmyoglobin

@ast

NMR evidence for slow collective motions in cyanometmyoglobin

@en

NMR evidence for slow collective motions in cyanometmyoglobin

@nl

type

label

NMR evidence for slow collective motions in cyanometmyoglobin

@ast

NMR evidence for slow collective motions in cyanometmyoglobin

@en

NMR evidence for slow collective motions in cyanometmyoglobin

@nl

prefLabel

NMR evidence for slow collective motions in cyanometmyoglobin

@ast

NMR evidence for slow collective motions in cyanometmyoglobin

@en

NMR evidence for slow collective motions in cyanometmyoglobin

@nl

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P1433

Nature structural biology

P1476

NMR evidence for slow collective motions in cyanometmyoglobin

@en

P2093

J H Prestegard

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

J M Flanagan

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

J R Tolman

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

M A Kennedy

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

P2860

Solution structure of carbonmonoxy myoglobin determined from nuclear magnetic resonance distance and chemical shift constraints

Hydrated myoglobin's anharmonic fluctuations are not primarily due to dihedral transitions

Dynamical transition of myoglobin revealed by inelastic neutron scattering.

Conformational substates in proteins.

Dynamics of proteins: elements and function.

Thermal diffuse X-ray scattering and its contribution to understanding protein dynamics.

Magnetic Field Dependence of Nitrogen−ProtonJSplittings in15N-Enriched Human Ubiquitin Resulting from Relaxation Interference and Residual Dipolar Coupling

Protein crystal dynamics studied by time-resolved analysis of X-ray diffuse scattering

P304

292-7

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

P31

scholarly article

P356

10.1038/NSB0497-292

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

P407

P433

4

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

P478

4

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

P577

1997-04-01T00:00:00Z

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P698

9095197

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