Linked Life Data

10984589

Source:http://linkedlifedata.com/resource/pubmed/id/10984589

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-11-3
pubmed:abstractText
It is demonstrated here how the secondary structure and dynamics of transmembrane helices, as well as surface residues, such as interhelical loops and N- or C-terminus of bacteriorhodopsin (bR) in purple membrane, can be determined at ambient temperature based on very simple (13)C-NMR measurements, together with a brief experimental background. In contrast to the static picture of bR, currently available from X-ray diffraction or cryo-electron microscopy, the structure consists of dynamically heterogeneous domains which undergo various types of local fluctuations with a frequency range of 10(2)--10 (8) Hz. The significance of this picture is discussed in relation to the biological function of this protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
1460
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
39-48
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Conformation and backbone dynamics of bacteriorhodopsin revealed by (13)C-NMR.
pubmed:affiliation
Department of Life Science, Faculty of Science, Himeji Institute of Technology, Harima Science Garden City, Kouto 3-chome, Kamigori, 678-1297, Hyogo, Japan. saito@sci.himeji-tech.ac.jp
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't