SITE-DIRECTED ISOTOPE LABELING AND FTIR SPECTROSCOPY OF BACTERIORHODOPSIN

被引：72
作者：
SONAR, S
LEE, CP
COLEMAN, M
PATEL, N
LIU, XM
MARTI, T
KHORANA, HG
RAJBHANDARY, UL
ROTHSCHILD, KJ
机构：
[1] BOSTON UNIV, DEPT PHYS, BOSTON, MA 02215 USA
[2] BOSTON UNIV, MOLEC BIOPHYS LAB, BOSTON, MA 02215 USA
[3] MIT, DEPT BIOL, CAMBRIDGE, MA 02139 USA
[4] MIT, DEPT CHEM, CAMBRIDGE, MA 02139 USA
来源：
NATURE STRUCTURAL BIOLOGY | 1994年 / 1卷 / 08期
关键词：
D O I：
10.1038/nsb0894-512
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：
Insight into Integral membrane proteins function is presently limited by the difficulty of producing three-dimensional crystals. In addition, X-ray structures Of proteins normally do not provide information about the protonation state and structural changes of individual residues, We report here the first use of Site-directed isotope labelling and Fourier transform infrared (FTIR) difference spectroscopy to detect structural changes at the level of single residues in an Integral membrane protein. Two site-directed Isotope labeled (SDIL) tyrosine analogues of bacteriorhodopsin were produced which exhibit normal activity. FTIR spectroscopy shows that out of 11 tyrosines, only Tyr 185 is structurally active during the early photocycle and may be part of a proton wire.
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收藏
页码：512 / 517
页数：6
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