Linked Life Data

14871121

Source:http://linkedlifedata.com/resource/pubmed/id/14871121

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2004-2-11
pubmed:abstractText
TROSY-based NMR relaxation dispersion experiments that measure the decay of double- and zero-quantum (1)H-(15)N coherences as a function of applied (1)H and (15)N radio frequency (rf) fields are presented for studying millisecond dynamic processes in proteins. These experiments are complementary to existing approaches that measure dispersions of single-quantum (15)N and (1)H magnetization. When combined, data from all four coherences provide a more quantitative picture of dynamics, making it possible to distinguish, for example, between two-site and more complex exchange processes. In addition, a TROSY-based pulse scheme is described for measuring the relaxation of amide (1)H single-quantum magnetization, obtained by a simple modification of the multiple-quantum experiments. The new methodology is applied to a point mutant of the Fyn SH3 domain that exchanges between folded and unfolded states at 25 degrees C.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
126
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1886-91
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Double- and zero-quantum NMR relaxation dispersion experiments sampling millisecond time scale dynamics in proteins.
pubmed:affiliation
Swedish NMR Center at Göteborg University, Box 465, 40530 Göteborg, Sweden. orov@nmr.se
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't