Assessing the functionality of a membrane protein in a three-dimensional crystal

被引：47

作者：

Heberle, J

Büldt, G

Koglin, E

Rosenbusch, JP

Landau, EM

机构：

[1] Forschungszentrum Julich, Inst Biol & Informationsverarbeitung, Struct Biol, D-52425 Julich, Germany

[2] Forschungszentrum Julich, Inst Chem & Dynam Geosphare, D-52425 Julich, Germany

[3] Univ Basel, Biozentrum, CH-4056 Basel, Switzerland

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1998年 / 281卷 / 04期

关键词：

FT-IR; time-resolved; proton transfer; bacteriorhodopsin; lipidic cubic phase crystallization;

D O I：

10.1006/jmbi.1998.1970

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：

Hexagonal microcrystals of bacteriorhodopsin embedded in a lipidic cubic phase have been investigated by time-resolved FT-IR and resonance Raman spectroscopy. Retinal isomerization, conformational changes in the protein backbone and proton translocation are virtually indistinguishable from those in the native membrane. The protein is thus fully active in three-dimensional crystals. (C) 1998 Academic Press.

引用

页码：587 / 592

页数：6

共 24 条

[21] CHROMOPHORE MOTION DURING THE BACTERIORHODOPSIN PHOTOCYCLE - POLARIZED ABSORPTION-SPECTROSCOPY OF BACTERIORHODOPSIN AND ITS M-STATE IN BACTERIORHODOPSIN CRYSTALS [J].