Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
2004-4-14
pubmed:abstractText
An enhanced sensitivity zero-quantum correlation experiment is proposed for recording (1)H-(13)C correlations of methyl groups in highly deuterated, methyl protonated large proteins. The zero-quantum spectra benefit from TROSY-effects in which both intra- and inter-methyl dipolar relaxation interactions are minimized. Applications to malate synthase G at 5 degrees C (81 kDa single polypeptide chain enzyme, correlation time of 118 ns) and lysine decarboxylase at 45 degrees C (810 kDa decameric enzyme) are presented showing significant improvements in resolution relative to corresponding HMQC data sets, with only slight decreases (approximately 10%) in sensitivity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
126
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4921-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Line narrowing in methyl-TROSY using zero-quantum 1H-13C NMR spectroscopy.
pubmed:affiliation
Protein Engineering Network Centers of Excellence and Department of Medical Genetics, The University of Toronto, Toronto, Ontario, Canada, M5S 1A8.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't