Linked Life Data

8672440

Source:http://linkedlifedata.com/resource/pubmed/id/8672440

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1996-8-13
pubmed:abstractText
Fourier transform infrared spectra of light-adapted bacteriorhodopsin exhibit a band at 1618 cm(-1) that shifts to 1625 cm(-1) upon formation of the L intermediate. It is assigned to the peptide C==O of Val49 from the fact that it shifts in [1-(13)C]valine-labeled bacteriorhodopsin and appears perturbed in the Val49-->Met mutant. The intensity of the BR-->L difference band is reduced in the Thr46-->Val mutant but restored by the additional mutation of Asp96-->Asn. These intensity changes are closely correlated with the H-bonding change of water olecules, suggesting that the peptide C==O of Val49 is hydrated. This could arise in the Thr46-->Val mutant because of perturbation of the C==O of Val46, which points toward Val49. The Val49-->Ala mutation influences a peptide N-H, presumably of Val49, and the carboxylic C==O of Asp96, as well as water molecules proximal to Asp85. Conversely, the water molecule assumed to be in the cavity that arises from the missing two methyl groups in V49A could be affected in the mutant of Asp96-->Asn. We propose that the perturbation exerted on Asp85 by the Schiff base in the L intermediate is transmitted to Asp96 through H-bonding of water molecules in the Asp85-Val49 region, the C==O of Val49, H-bonding between Val49 and Thr46, and H-bonding between Thr46 and Asp96.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4063-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Hydrogen bonds of water and C==O groups coordinate long-range structural changes in the L photointermediate of bacteriorhodopsin.
pubmed:affiliation
Department of Biophysics, Graduate School of Science, Kyoto University, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't