Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-7-19
pubmed:abstractText
Resonance patterns have been observed in 2D solid-state NMR spectra of the transmembrane segment of M2 protein from Influenza A virus in oriented samples reflecting the helical wheel of this alpha-helix. The center of this pattern uniquely defines the helical tilt with respect to the bilayer normal without a need for resonance assignments. The distribution of resonances from amino acid specific labels around the "PISA wheel" defines the rotational orientation of the helix and yields preliminary site-specific assignments. With assignments high-resolution structural detail, such as differences in tilt and rotational orientation along the helical axis leading to an assessment of helical coiling, can be obtained.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1090-7807
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:volume
144
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
162-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Imaging membrane protein helical wheels.
pubmed:affiliation
National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida 32310, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.