Linked Life Data

19319480

Source:http://linkedlifedata.com/resource/pubmed/id/19319480

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2009-8-18
pubmed:abstractText
Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion NMR experiments are extremely powerful for characterizing millisecond time-scale conformational exchange processes in biomolecules. A large number of such CPMG experiments have now emerged for measuring protein backbone chemical shifts of sparsely populated (>0.5%), excited state conformers that cannot be directly detected in NMR spectra and that are invisible to most other biophysical methods as well. A notable deficiency is, however, the absence of CPMG experiments for measurement of (1)H(alpha) and (13)C(alpha) chemical shifts of glycine residues in the excited state that reflects the fact that in this case the (1)H(alpha), (13)C(alpha) spins form a three-spin system that is more complex than the AX (1)H(alpha)-(13)C(alpha) spin systems in the other amino acids. Here pulse sequences for recording (1)H(alpha) and (13)C(alpha) CPMG relaxation dispersion profiles derived from glycine residues are presented that provide information from which (1)H(alpha), (13)C(alpha) chemical shifts can be obtained. The utility of these experiments is demonstrated by an application to a mutant of T4 lysozyme that undergoes a millisecond time-scale exchange process facilitating the binding of hydrophobic ligands to an internal cavity in the protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1573-5001
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
45-55
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
CPMG relaxation dispersion NMR experiments measuring glycine 1H alpha and 13C alpha chemical shifts in the 'invisible' excited states of proteins.
pubmed:affiliation
Departments of Molecular Genetics, Biochemistry and Chemistry, University of Toronto, Toronto, Ontario, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't