Linked Life Data

6487621

Source:http://linkedlifedata.com/resource/pubmed/id/6487621

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1984-11-28
pubmed:abstractText
The 21 amino acids which can be selectively removed from the carboxyl terminus of bacteriorhodopsin by proteolytic treatment are disordered in 2-dimensional arrays of the protein present in purple membranes. This C-terminal portion of the molecule may be involved in the efficiency and rate of light-driven proton uptake, although its presence is not required for pumping activity. In this study, the secondary structure of the C-terminus of bacteriorhodopsin has been determined by examining circular dichroism (CD) difference spectra derived from native and digested samples. In low ionic strength media, this part of the molecule appears to form a random coil-like structure. To examine if this structure is related to the structure found under the high ionic strength condition present in halobacteria, the CD spectra of native purple membranes in water and in 4 M salt solutions were compared. They were found to be identical, suggesting the conformation of the C-terminus in vivo may also be a random coil.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
777
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
93-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
The C-terminus of bacteriorhodopsin is a random coil.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't