About: TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins

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article by Michael Salzmann et al published February 1999 in Journal of the American Chemical Society

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в лютому 1999 (uk) article scientifique publié en 1999 (fr) im Februar 1999 veröffentlichter wissenschaftlicher Artikel (de) article by Michael Salzmann et al published February 1999 in Journal of the American Chemical Society (en)
publication date	wds:Q57825764-7D7DDFC7-E0F7-45B7-B459-B8878D0CFFAF
publication date	1999-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57825764-774EB009-B062-468A-A1D7-ADF2FB749C1C
language of work or name	English
cites work	wds:Q57825764-0C4706C4-3CF7-4EAE-8D0B-ADC0DAEC9095 wds:Q57825764-161AFDCE-F645-4209-B722-177F0952DEE0 wds:Q57825764-38F5CAA0-DFE5-438F-A87C-C7AB27C505F6 wds:Q57825764-43C9EBB5-D1A8-488E-972C-CE5FEBF22404 wds:Q57825764-83B1FF75-5A6D-4FBF-91D6-89DD7F0E86F1 wds:Q57825764-89C71EA0-F31F-4C0A-963E-9B38F67520BB wds:Q57825764-8DB3D4EB-068B-4DE7-BDF8-2709FB185AFA wds:Q57825764-AEA0E55A-2333-4733-9350-0FFD644DD129 wds:Q57825764-C68219B4-3A06-489B-8E1E-C2BBFA52C64C wds:Q57825764-EC87B911-DE4B-4990-9AEA-0AAF6F5C91F0 wds:Q57825764-F31A09DD-51CE-40DE-85F7-6FE687D55631
cites work	Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR Technical aspects of NMR Spectroscopy with biological macromolecules and studies of hydration in solution Processing of multi-dimensional NMR data with the new software PROSA 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 Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance Transverse Relaxation-Optimized Spectroscopy (TROSY) for NMR Studies of Aromatic Spin Systems in13C-Labeled Proteins Single Transition-to-single Transition Polarization Transfer (ST2-PT) in [15N,1H]-TROSY. TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins Structure and mechanism of DNA topoisomerases. A sensitive HN(CA)CO experiment for deuterated proteins
author name string	wds:Q57825764-70024334-DB3C-4FE8-83E2-6E7E2A6D3A93 wds:Q57825764-A145AF59-EEE2-472C-ACC6-BFD95C877EC6 wds:Q57825764-C5CFF244-B90B-410E-A4C6-8538DA2D83DF
author name string	Konstantin Pervushin Hans Senn Michael Salzmann
rdfs:label	TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins (en) TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins (nl)
skos:prefLabel	TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins (en) TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins (nl)
name	TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins (en) TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins (nl)
author	wds:Q57825764-85F41127-C150-477D-B44B-8AE032E516DD wds:Q57825764-E20370F5-2D8D-4006-BA08-80A6D3262C6F
author	Kurt Wüthrich Gerhard Wider
title	wds:Q57825764-BE68C73F-EF46-42A6-8FCB-BF8FF9536E0C
title	TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins (en)
page(s)	wds:Q57825764-3A4B523A-0EB5-40FE-BB35-9EF88AE24E06
page(s)	844-848
instance of	wds:Q57825764-1DA3955B-7E08-430D-9F0B-A4060A6A4114
instance of	scholarly article
published in	wds:Q57825764-EAEC170A-8F14-42C8-95AA-162CD3294D3C
published in	Journal of the American Chemical Society
issue	wds:Q57825764-4DFCFA42-F520-462A-877D-86344BC5C5EF
volume	wds:Q57825764-E215A14B-949F-4464-97B6-A2204CC824A6
issue	4
volume	121
DOI	wds:Q57825764-9F1D2837-3113-48EE-B1DF-235D4402A202
DOI	http://dx.doi.org/10.1021/JA9834226
DOI	10.1021/JA9834226
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57825764
is cites work of	Quaternary structure of hemoglobin in solution Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction. NMR spectroscopy of large molecules and multimolecular assemblies in solution. Structure of the C3b binding site of CR1 (CD35), the immune adherence receptor Proton-proton Overhauser NMR spectroscopy with polypeptide chains in large structures The Apo-structure of the Low Molecular Weight Protein-tyrosine Phosphatase A (MptpA) from Mycobacterium tuberculosis Allows for Better Target-specific Drug Development The role of the Src homology 3-Src homology 2 interface in the regulation of Src kinases Solution structure and stability of the full-length excisionase from bacteriophage HK022 Solution NMR studies of an intrinsically unstructured protein within a dilute, 75 kDa eukaryotic protein assembly; probing the practical limits for efficiently assigning polypeptide backbone resonances. Solution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from Escherichia coli NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors Structural characterization of the nickel-binding properties of Bacillus pasteurii urease accessory protein (Ure)E in solution Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45 NMR Backbone Assignment of Large Proteins by Using (13) Cα -Only Triple-Resonance Experiments Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles Effects of NMR spectral resolution on protein structure calculation NMR techniques used with very large biological macromolecules in solution Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data NMR solution structure determination of RNAs NMR structure of the heme chaperone CcmE reveals a novel functional motif Facile backbone structure determination of human membrane proteins by NMR spectroscopy NMR solution structure determination of membrane proteins reconstituted in detergent micelles Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli Transmembrane segment enhanced labeling as a tool for the backbone assignment of alpha-helical membrane proteins NMR resonance assignments of thrombin reveal the conformational and dynamic effects of ligation. The solution structure of EMILIN1 globular C1q domain reveals a disordered insertion necessary for interaction with the alpha4beta1 integrin NMR analysis of a 900K GroEL GroES complex Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain Biophysical approaches to membrane protein structure determination TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution. The Rac1 polybasic region is required for interaction with its effector PRK1 Overview on the use of NMR to examine protein structure NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol The glucocorticoid receptor dimer interface allosterically transmits sequence-specific DNA signals Cluster and fold stability of E. coli ISC-type ferredoxin Direct comparison of a stable isolated Hsp70 substrate-binding domain in the empty and substrate-bound states

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