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Solution NMR of supramolecular complexes: providing new insights into function
scientific article published on 01 September 2007
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Europe PubMed Central
PubMed publication ID
17762877
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17762877%20AND%20SRC:MED&resulttype=core&format=json
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4 January 2020
title
Solution NMR of supramolecular complexes: providing new insights into function
(English)
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Europe PubMed Central
PubMed publication ID
17762877
reference URL
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4 January 2020
author name string
Remco Sprangers
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1
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Europe PubMed Central
PubMed publication ID
17762877
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4 January 2020
Algirdas Velyvis
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2
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Europe PubMed Central
PubMed publication ID
17762877
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Lewis E Kay
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3
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PubMed publication ID
17762877
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4 January 2020
publication date
1 September 2007
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PubMed publication ID
17762877
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4 January 2020
published in
Nature Methods
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Europe PubMed Central
PubMed publication ID
17762877
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17762877%20AND%20SRC:MED&resulttype=core&format=json
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4 January 2020
volume
4
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Europe PubMed Central
PubMed publication ID
17762877
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17762877%20AND%20SRC:MED&resulttype=core&format=json
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4 January 2020
issue
9
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PubMed publication ID
17762877
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4 January 2020
page(s)
697-703
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PubMed publication ID
17762877
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4 January 2020
exact match
https://scigraph.springernature.com/pub.10.1038/nmeth1080
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Weak alignment offers new NMR opportunities to study protein structure and dynamics.
1 reference
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Crossref
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7 January 2021
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NMR spectroscopy of large molecules and multimolecular assemblies in solution.
1 reference
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Crossref
reference URL
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7 January 2021
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The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins
1 reference
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Crossref
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7 January 2021
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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
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NMR analysis of a 900K GroEL GroES complex
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7 January 2021
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Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
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7 January 2021
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Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution
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Solution NMR-derived global fold of a monomeric 82-kDa enzyme
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New tools provide new insights in NMR studies of protein dynamics
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7 January 2021
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New developments in isotope labeling strategies for protein solution NMR spectroscopy
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Crossref
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Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy
1 reference
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NMR sequential assignment of Escherichia coli thioredoxin utilizing random fractional deuteriation
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Carbon-13 line narrowing by deuterium decoupling in deuterium/carbon-13/nitrogen-15 enriched proteins. Application to triple resonance 4D J connectivity of sequential amides
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An isotope labeling strategy for methyl TROSY spectroscopy
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Surface, subunit interfaces and interior of oligomeric proteins
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Global Folds of Highly Deuterated, Methyl-Protonated Proteins by Multidimensional NMR†
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Automated protein fold determination using a minimal NMR constraint strategy
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Dynamics of methyl groups in proteins as studied by proton-detected 13C NMR spectroscopy. Application to the leucine residues of staphylococcal nuclease
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Quantitative 13C and 2H NMR relaxation studies of the 723-residue enzyme malate synthase G reveal a dynamic binding interface
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A robust and cost-effective method for the production of Val, Leu, Ile (delta 1) methyl-protonated 15N-, 13C-, 2H-labeled proteins
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Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution
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Oligopeptide biases in protein sequences and their use in predicting protein coding regions in nucleotide sequences
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Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes
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7 January 2021
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Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release
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7 January 2021
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Quantitative dynamics and binding studies of the 20S proteasome by NMR
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7 January 2021
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7 January 2021
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A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase
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Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP.
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Control of peptide product sizes by the energy-dependent protease ClpAP.
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A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium
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Solution NMR spin relaxation methods for characterizing chemical exchange in high-molecular-weight systems
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Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: application to a 723-residue enzyme
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7 January 2021
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Identifiers
DOI
10.1038/NMETH1080
1 reference
stated in
Europe PubMed Central
PubMed publication ID
17762877
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17762877%20AND%20SRC:MED&resulttype=core&format=json
retrieved
4 January 2020
Dimensions Publication ID
1013631003
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PubMed publication ID
17762877
1 reference
stated in
Europe PubMed Central
PubMed publication ID
17762877
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17762877%20AND%20SRC:MED&resulttype=core&format=json
retrieved
4 January 2020
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