About: Single-Step Determination of Protein Substructures Using Dipolar Couplings: Aid to Structural Genomics

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scientific article published on 01 September 2001

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована у вересні 2001 (uk) article scientifique publié en 2001 (fr) im September 2001 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en setiembre de 2001 (ast) scientific article published on 01 September 2001 (en)
publication date	wds:Q57211407-C9339BA1-0DC3-4325-9548-69077C832E8F
publication date	2001-09-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57211407-834D8144-922C-4960-8D62-6BED2BE66495
language of work or name	English
rdfs:label	Single-Step Determination of Protein Substructures Using Dipolar Couplings: Aid to Structural Genomics (en) Single-Step Determination of Protein Substructures Using Dipolar Couplings: Aid to Structural Genomics (nl)
skos:prefLabel	Single-Step Determination of Protein Substructures Using Dipolar Couplings: Aid to Structural Genomics (en) Single-Step Determination of Protein Substructures Using Dipolar Couplings: Aid to Structural Genomics (nl)
name	Single-Step Determination of Protein Substructures Using Dipolar Couplings: Aid to Structural Genomics (en) Single-Step Determination of Protein Substructures Using Dipolar Couplings: Aid to Structural Genomics (nl)
author	wds:Q57211407-1714BF28-348D-4947-8BCA-7DD185E514FF wds:Q57211407-B3F8F884-526E-403D-ABF8-6F7B454BBF6B
author	Ad Bax Markus Zweckstetter
title	wds:Q57211407-EC2128C4-691E-40F3-9256-EA9CBDD58EE4
title	Single-step determination of protein substructures using dipolar couplings: aid to structural genomics (en)
page(s)	wds:Q57211407-6B858FDD-EF0C-48BE-93DB-3AB166E832DD
page(s)	9490-9491
instance of	wds:Q57211407-307EA22D-A8D8-48A3-A6EA-E40D6D27CBAA
instance of	scholarly article
main subject	wds:Q57211407-9A396001-48CF-4870-8D3D-7284C28259B5
main subject	genomics
PubMed ID	wds:Q57211407-EE6FA649-45BC-4B03-9681-47B8AF714B19
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11562251
PubMed ID	11562251
published in	wds:Q57211407-68EDA7A0-FE1D-4660-942B-08DF5B6E55ED
published in	Journal of the American Chemical Society
issue	wds:Q57211407-962CECF6-2CE4-49C3-99AA-26915068210A
volume	wds:Q57211407-16168547-20A0-4F99-84F3-17D54FF39C45
issue	38
volume	123
DOI	wds:Q57211407-25BB1D7D-9B5D-4D41-A2BE-4AB437C7527A
DOI	http://dx.doi.org/10.1021/JA016496H
DOI	10.1021/JA016496H
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57211407
is cites work of	NMR solution structure and backbone dynamics of domain III of the E protein of tick-borne Langat flavivirus suggests a potential site for molecular recognition Biophysical characterization of naturally occurring titin M10 mutations Structural polymorphism of 441-residue tau at single residue resolution Magnetically aligned phospholipid bilayers in weak magnetic fields: optimization, mechanism, and advantages for X-band EPR studies GFT NMR experiments for polypeptide backbone and 13Cbeta chemical shift assignment. Role for NMR in structural genomics Backbone 1H, 15N and 13C assignments for the 21 kDa Caenorhabditis elegans homologue of "brain-specific" protein Weak alignment offers new NMR opportunities to study protein structure and dynamics. Structural Characterization of a Mannose-binding Protein–Trimannoside Complex using Residual Dipolar Couplings A structural model for the single-stranded DNA genome of filamentous bacteriophage Pf1. Dipolar waves as NMR maps of protein structure Blind testing of routine, fully automated determination of protein structures from NMR data Assignment validation software suite for the evaluation and presentation of protein resonance assignment data Intrinsically disordered proteins: from sequence and conformational properties toward drug discovery Molecular fragment replacement approach to protein structure determination by chemical shift and dipolar homology database mining. Protein sequential resonance assignments by combinatorial enumeration using 13C alpha chemical shifts and their (i, i-1) sequential connectivities The intermembrane space domain of Tim23 is intrinsically disordered with a distinct binding region for presequences High-throughput screening of structural proteomics targets using NMR. 4D non-uniformly sampled HCBCACON and ¹J(NCα)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins The conserved CPH domains of Cul7 and PARC are protein-protein interaction modules that bind the tetramerization domain of p53 5D 13C-detected experiments for backbone assignment of unstructured proteins with a very low signal dispersion Theoretical and computational advances in biomolecular NMR spectroscopy Measurement of long range H,C couplings in natural products in orienting media: a tool for structure elucidation of natural products Determination of protein global folds using backbone residual dipolar coupling and long-range NOE restraints. An expectation/maximization nuclear vector replacement algorithm for automated NMR resonance assignments. Towards structural genomics of RNA: rapid NMR resonance assignment and simultaneous RNA tertiary structure determination using residual dipolar couplings Determination of molecular alignment tensors without backbone resonance assignment: Aid to rapid analysis of protein-protein interactions Automated NMR Assignment and Protein Structure Determination using Sparse Dipolar Coupling Constraints. Backbone assignment of proteins with known structure using residual dipolar couplings Function first: a powerful approach to post-genomic drug discovery RDC derived protein backbone resonance assignment using fragment assembly. Extended Experimental Inferential Structure Determination Method in Determining the Structural Ensembles of Disordered Protein States Current Awareness on Comparative and Functional Genomics Improved validation of IDP ensembles by one-bond Cα-Hα scalar couplings. HMGB1-carbenoxolone interactions: dynamics insights from combined nuclear magnetic resonance and molecular dynamics.
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