About: Ultrahigh-Resolution Backbone Structure of Perdeuterated Protein GB1 Using Residual Dipolar Couplings from Two Alignment Media

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scholarly article by Guillaume Bouvignies et al published 11 December 2006 in Angewandte Chemie International Edition

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rdf:type	Item
description	наукова стаття, опублікована в грудні 2006 (uk) im Dezember 2006 veröffentlichter wissenschaftlicher Artikel (de) scholarly article by Guillaume Bouvignies et al published 11 December 2006 in Angewandte Chemie International Edition (en)
publication date	wds:Q57080208-8DABD4DA-E79B-4160-B199-3CFDD46C9248
publication date	2006-12-11 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57080208-7FF7BDA0-D125-4185-B77B-C7EDF9F8ABC1
language of work or name	English
rdfs:label	Ultrahigh-Resolution Backbone Structure of Perdeuterated Protein GB1 Using Residual Dipolar Couplings from Two Alignment Media (en)
skos:prefLabel	Ultrahigh-Resolution Backbone Structure of Perdeuterated Protein GB1 Using Residual Dipolar Couplings from Two Alignment Media (en)
name	Ultrahigh-Resolution Backbone Structure of Perdeuterated Protein GB1 Using Residual Dipolar Couplings from Two Alignment Media (en)
author	wds:Q57080208-0B7268D4-468C-4E8C-9309-12053CF37DD1 wds:Q57080208-817D4A76-21BF-41B5-9F72-635571B1949B wds:Q57080208-A49AC629-FA48-4609-A3CB-C2AEA92C1FCB wds:Q57080208-C711B9D7-ADD0-4661-986B-5FD48953C067
author	Martin Blackledge Stephan Grzesiek Sebastian Meier Guillaume Bouvignies
title	wds:Q57080208-76B39830-5E8D-46E6-BC88-D1AF0D795F19
title	Ultrahigh-Resolution Backbone Structure of Perdeuterated Protein GB1 Using Residual Dipolar Couplings from Two Alignment Media (en)
page(s)	wds:Q57080208-478F53BC-8603-41C6-872C-C13D81B73243
page(s)	8166-8169
instance of	wds:Q57080208-ABA8CB8E-91ED-428D-A92F-69DD2D3F7392
instance of	scholarly article
main subject	wds:Q57080208-0B0526DE-5B83-4207-871A-3D4C49430050 wds:Q57080208-5081194F-0FF9-4A9A-8243-8BCFADF62501 wds:Q57080208-E6503A08-0EB4-483B-B528-FD046F1B5D42
main subject	general chemistry catalysis protein structure
PubMed ID	wds:Q57080208-397594E3-D318-452C-87FA-3A79B21E6B82
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/17120284
PubMed ID	17120284
published in	wds:Q57080208-2CB0167E-0EDA-4885-886A-8DC1B91A42CD
published in	Angewandte Chemie International Edition
issue	wds:Q57080208-FC928803-4598-4B95-A243-4DEDCE74D20C
volume	wds:Q57080208-C6048E0F-2670-41FA-B1FC-E9832ECF65F7
issue	48
volume	45
DOI	wds:Q57080208-A0E66B89-EF5D-426A-AEDE-84BB447E87B9
DOI	http://dx.doi.org/10.1002/ANIE.200603627
DOI	10.1002/ANIE.200603627
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57080208
is cites work of	Correlated motions are a fundamental property of β-sheets. Multi-timescale conformational dynamics of the SH3 domain of CD2-associated protein using NMR spectroscopy and accelerated molecular dynamics Top-down approach in protein RDC data analysis: de novo estimation of the alignment tensor. Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N-15N and carbonyl 13C-13C dipolar recoupling data Cysteine-specific Cu2+ chelating tags used as paramagnetic probes in double electron electron resonance. Simultaneous definition of high resolution protein structure and backbone conformational dynamics using NMR residual dipolar couplings. Mapping protein conformational energy landscapes using NMR and molecular simulation. Flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables. Protein loop closure using orientational restraints from NMR data Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons. Inferring protein 3D structure from deep mutation scans An improved algorithm for MFR fragment assembly Automated robust and accurate assignment of protein resonances for solid state NMR. Measurement of Structural Restraints VirtualSpectrum, a tool for simulating peak list for multi-dimensional NMR spectra Smad7 Binds Differently to Individual and Tandem WW3 and WW4 Domains of WWP2 Ubiquitin Ligase Isoforms
is cites work of	wds:Q30363082-6098E1F1-A247-4DAD-A939-822A2D439770 wds:Q34208232-0BE9C8BC-ECF7-4432-8CC9-451FB66419B5 wds:Q92826872-33CD59B1-5AF3-4AD4-89A0-136149E9077A wds:Q30010111-F37E5082-3CE9-47FA-9D76-6C81406B8C5F wds:Q30362591-933F3134-516D-43FF-B82C-CBC4A4896215 wds:Q34267144-0B95773E-F307-480E-B7A7-B92538EB9E9E wds:Q30370965-D63A1DA9-0440-4E8B-AA92-94BD092FDC89 wds:Q34097299-D58BB68C-7879-497D-B4F3-1F5FEF948A3F wds:Q50963890-BB86C14D-FFC6-4332-AE3B-48BB405DADDA wds:Q43692806-4CA4FA35-CAD1-4E3C-ADDB-6F1A78E0E47B wds:Q30360240-57D6233D-D178-4A3D-9455-B03B6E15E562 wds:Q44399746-46D05A07-E449-49F5-AE3F-B77BFE8B647F wds:Q47734327-87AB987A-9361-46F3-8CB3-49437C4A1D41 wds:Q57080179-BF651661-F81D-4FE9-A2EB-3D9A464A3199 wds:Q90223957-12E90767-C228-4E37-A9A0-C10B7D6D83BC wds:Q46735392-D4382A89-141B-4BE1-A757-016EF557DAEB

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