Molecular reaction mechanisms of proteins monitored by time-resolved FTIR-spectroscopy

被引:75
作者
Gerwert, K [1 ]
机构
[1] Ruhr Univ Bochum, Lehrstuhl Biophys, D-44780 Bochum, Germany
关键词
bacteriorhodopsin; caged GTP; FTIR; H-ras p21; proton transfer;
D O I
10.1515/BC.1999.115
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
Time-resolved FTIR difference spectroscopy can provide a valuable insight into the molecular reaction mechanisms of proteins, especially membrane proteins. Isotopic labeling and site-directed mutagenesis allows an unequivocal assignment of IR absorption bands. Studies are presented which give insight into the proton pump mechanisms of proteins, especially bacteriorhodopsin, H-bonded network proton transfer via internal water molecules seems to be a general feature in proteins, also found in cytochrome c oxidase. Using caged GTP the intrinsic and GAP catalyzed GTPase activity of H-ras p21 is studied. Furthermore, protein folding reactions can be recorded with ns time-resolution.
引用
收藏
页码:931 / 935
页数:5
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