Linked Life Data

15140426

Source:http://linkedlifedata.com/resource/pubmed/id/15140426

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-5-13
pubmed:abstractText
Transmembrane helices are more uniform in structure than similar helices in water soluble proteins. Solid state NMR of aligned bilayer samples is being increasingly used to characterize helical membrane protein structures. Traditional spectroscopic methods have difficulty distinguishing between helices with i to i + 3 (3(10)), i to i + 4 (alpha), and i to i + 5 (pi) hydrogen bonding topology. Here, we show that resonance patterns in PISEMA spectra simulated for these different helices show unique and striking features. The size and shape of these Polar Index Slant Angle (PISA) wheels, as well as the resonances per turn and clockwise versus counter-clockwise sequential connectivity of the resonances demonstrate how these different helical structures, if present as a uniform structure, will be readily distinguished, and characterized.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1090-7807
pubmed:author
pubmed:issnType
Print
pubmed:volume
168
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
187-93
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
2D solid state NMR spectral simulation of 3(10), alpha, and pi-helices.
pubmed:affiliation
National High Magnetic Field Laboratory, Institute of Molecular Biophysics, Tallahassee, FL 32310, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S., Evaluation Studies, Validation Studies