Elucidation of the ultrafast isomerization mechanism of rhodopsin, a photoreceptor protein present in vertebrates, has been one of the central focuses of vision as well as ultrafast spectroscopy. Upon absorption of light by 11-cis retinal, the cofactor in rhodopsin, an ultrafast isomerization reaction takes place with high efficiency, 67%, to form all-trans retinal. In this project, we plan to study some rhodopsin analogues which contain 11-cis-locked-ring retinals with five-, seven-, and eight-membered rings. They have been shown to reconstitute with opsin and possess similar ground state absorption spectra as the native system. Previous work by Nakanishi and coworkers has shown that the retinal analogues undergo isomerization to a limited extent depending upon the ring size. We plan to investigate the transient anisotropy signals from these systems in the hope that they will help us better understand the anisotropy response we have previously observed in native rhodopsi n. These systems should be much easier to work with since they do not undergo permanent photobleaching like the native system.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001348-19
Application #
6328046
Study Section
Project Start
2000-08-01
Project End
2001-07-31
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
19
Fiscal Year
2000
Total Cost
$2,726
Indirect Cost
Name
University of Pennsylvania
Department
Type
DUNS #
042250712
City
Philadelphia
State
PA
Country
United States
Zip Code
19104
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