Linked Life Data

21626214

Source:http://linkedlifedata.com/resource/pubmed/id/21626214

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2011-7-12
pubmed:abstractText
Obtaining sequence-specific assignments remains a major bottleneck in solution NMR investigations of supramolecular structure, dynamics and interactions. Here we demonstrate that resonance assignment of methyl probes in high molecular weight protein assemblies can be efficiently achieved by combining fast NMR experiments, residue-type-specific isotope-labeling and automated site-directed mutagenesis. The utility of this general and straightforward strategy is demonstrated through the characterization of intermolecular interactions involving a 468-kDa multimeric aminopeptidase, PhTET2.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1573-5001
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
229-36
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
pubmed:affiliation
Institut de Biologie Structurale Jean-Pierre Ebel, CNRS, Grenoble, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't