About: Probing Chemical Shifts of Invisible States of Proteins with Relaxation Dispersion NMR Spectroscopy: How Well Can We Do?

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Probing Chemical Shifts of Invisible States of Proteins with Relaxation Dispersion NMR Spectroscopy: How Well Can We Do? Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific article published on 01 February 2008

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) article scientifique publié en 2008 (fr) наукова стаття, опублікована в лютому 2008 (uk) im Februar 2008 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en febreru de 2008 (ast) artikull shkencor i botuar më 01 shkurt 2008 (sq) scientific article published on 01 February 2008 (en)
publication date	wds:Q59102877-8F82B5E1-0EA4-41F2-8082-EF8E0D1D7958
publication date	2008-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59102877-B4A84068-024F-4B4E-8641-EC3213976629
language of work or name	English
author name string	wds:Q59102877-5CA0E998-8A50-476F-9E28-876064336683 wds:Q59102877-6649B4B3-2234-4442-8E96-17B6FC6EA5C5
author name string	Pramodh Vallurupalli Patrik Lundström
rdfs:label	Probing Chemical Shifts of Invisible States of Proteins with Relaxation Dispersion NMR Spectroscopy: How Well Can We Do? (en) Probing Chemical Shifts of Invisible States of Proteins with Relaxation Dispersion NMR Spectroscopy: How Well Can We Do? (nl) Probing Chemical Shifts of Invisible States of Proteins with Relaxation Dispersion NMR Spectroscopy: How Well Can We Do? (sq)
skos:prefLabel	Probing Chemical Shifts of Invisible States of Proteins with Relaxation Dispersion NMR Spectroscopy: How Well Can We Do? (en) Probing Chemical Shifts of Invisible States of Proteins with Relaxation Dispersion NMR Spectroscopy: How Well Can We Do? (nl) Probing Chemical Shifts of Invisible States of Proteins with Relaxation Dispersion NMR Spectroscopy: How Well Can We Do? (sq)
name	Probing Chemical Shifts of Invisible States of Proteins with Relaxation Dispersion NMR Spectroscopy: How Well Can We Do? (en) Probing Chemical Shifts of Invisible States of Proteins with Relaxation Dispersion NMR Spectroscopy: How Well Can We Do? (nl) Probing Chemical Shifts of Invisible States of Proteins with Relaxation Dispersion NMR Spectroscopy: How Well Can We Do? (sq)
author	wds:Q59102877-330ADEBD-93F3-40F7-8D49-79FB7E2BA14E wds:Q59102877-576FA2D1-9F5F-4BDB-8452-288710650769 wds:Q59102877-8220F4B5-1A33-45E9-9285-86FA5B7662DC
author	Lewis E. Kay Philipp Neudecker Flemming Hansen
title	wds:Q59102877-1F51EE13-C470-40F1-B7A3-E874DC5B4F5E
title	Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy: how well can we do? (en)
page(s)	wds:Q59102877-2CDE8987-FD36-42A5-8D2B-581EAE895B65
page(s)	2667-2675
instance of	wds:Q59102877-1F57CD45-3EFB-46A4-9FEF-D3815D780073
instance of	scholarly article
main subject	wds:Q59102877-4382FDB5-7059-45FA-BC50-F728EF250659 wds:Q59102877-67CD5EF7-ADF9-4B4E-A0F3-2AC6DE6209F9
main subject	NMR spectroscopy spectroscopy
PubMed ID	wds:Q59102877-63E80ED6-E279-472E-9862-3304745DA2D4
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18237174
PubMed ID	18237174
published in	wds:Q59102877-9C0E638A-F3D3-4BB0-8D38-54AAAD968BA5
published in	Journal of the American Chemical Society
issue	wds:Q59102877-2DF6C02B-670B-46E8-AC13-3045D37BCBE4
volume	wds:Q59102877-8A4C25E1-BC4D-43FA-A516-ACCCFAE0E30C
issue	8
volume	130
DOI	wds:Q59102877-541E6A67-655D-420A-BBA2-66CBC4F730AE
DOI	http://dx.doi.org/10.1021/JA078337P
DOI	10.1021/JA078337P
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59102877
is cites work of	Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic NMR spectroscopy brings invisible protein states into focus Solution structure of a minor and transiently formed state of a T4 lysozyme mutant Chemical exchange in biomacromolecules: past, present, and future Structure and dynamic properties of membrane proteins using NMR. Probing microsecond time scale dynamics in proteins by methyl (1)H Carr-Purcell-Meiboom-Gill relaxation dispersion NMR measurements. Application to activation of the signaling protein NtrC(r) A simple method for measuring signs of (1)H (N) chemical shift differences between ground and excited protein states Isotope labeling methods for studies of excited protein states by relaxation dispersion NMR spectroscopy Measuring 13Cbeta chemical shifts of invisible excited states in proteins by relaxation dispersion NMR spectroscopy. 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 Visualizing transient dark states by NMR spectroscopy. Protein dynamics and function from solution state NMR spectroscopy Selective backbone labeling of proteins using 1,2-13C2-pyruvate as carbon source. Probing slowly exchanging protein systems via ¹³Cα-CEST: monitoring folding of the Im7 protein Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy Dynamics of ligand binding from 13C NMR relaxation dispersion at natural abundance A transient and low-populated protein-folding intermediate at atomic resolution relax: the analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. Exploration of the Conformational Dynamics of Major Histocompatibility Complex Molecules Evidence for dynamics in proteins as a mechanism for ligand dissociation Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis. Folding of the four-helix bundle FF domain from a compact on-pathway intermediate state is governed predominantly by water motion Hsp70 biases the folding pathways of client proteins Chemical shifts in biomolecules Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively (13)C labeled samples Measurement of signs of chemical shift differences between ground and excited protein states: a comparison between H(S/M)QC and R1rho methods Evaluating the influence of initial magnetization conditions on extracted exchange parameters in NMR relaxation experiments: applications to CPMG and CEST. Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study Mapping protein conformational energy landscapes using NMR and molecular simulation. Conformational exchange of aromatic side chains characterized by L-optimized TROSY-selected ¹³C CPMG relaxation dispersion Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups Evaluating the uncertainty in exchange parameters determined from off-resonance R1ρ relaxation dispersion for systems in fast exchange Crystallographic and Nuclear Magnetic Resonance Evaluation of the Impact of Peptide Binding to the Second PDZ Domain of Protein Tyrosine Phosphatase 1E Simultaneous detection and deconvolution of congested NMR spectra containing three isotopically labeled species Fractional enrichment of proteins using [2-(13)C]-glycerol as the carbon source facilitates measurement of excited state 13Cα chemical shifts with improved sensitivity Binding kinetics of histone chaperone Chz1 and variant histone H2A.Z-H2B by relaxation dispersion NMR spectroscopy Interaction Networks in Protein Folding via Atomic-Resolution Experiments and Long-Time-Scale Molecular Dynamics Simulations CPMG relaxation dispersion NMR experiments measuring glycine 1H alpha and 13C alpha chemical shifts in the 'invisible' excited states of proteins A computational study of the effects of (13) C-(13) C scalar couplings on (13) C CEST NMR spectra: towards studies on a uniformly (13) C-labeled protein When fast is better: protein folding fundamentals and mechanisms from ultrafast approaches Dynamics on multiple timescales in the RNA-directed RNA polymerase from the cystovirus phi6 An introduction to biological NMR spectroscopy Probing Protein-Protein Interactions Using Asymmetric Labeling and Carbonyl-Carbon Selective Heteronuclear NMR Spectroscopy Studying sparsely populated conformational states in RNA combining chemical synthesis and solution NMR spectroscopy.

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 176 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software