Linked Life Data

8873590

Source:http://linkedlifedata.com/resource/pubmed/id/8873590

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
41
pubmed:dateCreated
1996-11-27
pubmed:abstractText
Structural changes in the complex formation between transducin and metarhodopsin II, the activated form of photolyzed rhodopsin, in visual transduction processes were analyzed by Fourier transform infrared spectroscopy. The spectrum of the complex was obtained by subtracting the contribution of metarhodopsin I and uncomplexed metarhodopsin II. The averaged spectrum upon the complex formation was then compared with that in the conversion of rhodopsin-to-metarhodopsin II. Frequency shifts of the peptide carbonyl vibrations at 1686, 1674, and 1661 cm-1 to 1640 cm-1 were observed upon complex formation from metarhodopsin II plus transducin. These changes must have resulted from the strengthening of H-bonding of one or a few peptide groups but is not ascribable to global conformation change. Changes in the frequencies of the peptide amides were also detected. With regard to intramembrane carboxylic acid residues, no further changes were noticed in the carboxyl vibrations of Asp83, Glu122, and Glu113. Only a small change possibly due to Glu134 was detected.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13267-71
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Structural changes in the peptide backbone in complex formation between activated rhodopsin and transducin studied by FTIR spectroscopy.
pubmed:affiliation
Department of Biophysics, Graduate School of Science, Kyoto University, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't