CONFORMATIONAL-CHANGES IN RHODOPSIN PROBED BY SURFACE-PLASMON RESONANCE SPECTROSCOPY

被引:75
|
作者
SALAMON, Z
WANG, Y
BROWN, MF
MACLEOD, HA
TOLLIN, G
机构
[1] UNIV ARIZONA,DEPT BIOCHEM,TUCSON,AZ 85721
[2] UNIV ARIZONA,DEPT CHEM,TUCSON,AZ 85721
[3] UNIV ARIZONA,CTR OPT SCI,TUCSON,AZ 85721
关键词
D O I
10.1021/bi00250a022
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Surface plasmon resonance (SPR) spectroscopy has been used to follow incorporation and light-induced conformational changes in bovine rhodopsin reconstituted into an egg phosphatidylcholine bilayer deposited on a thin silver film. The magnitude of the SPR spectral changes caused by light varies with pH in a manner paralleling that in flash photolysis experiments, which monitor formation of metarhodopsin II. Irradiation produces an increase of approximately 4 Angstrom in the average thickness of the proteolipid layer, consistent with exposure of recognition sites for the G protein. The results demonstrate that the SPR technology described herein may be used to monitor conformational events in membrane-associated receptors such as rhodopsin.
引用
收藏
页码:13706 / 13711
页数:6
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