Effect of single-site mutation at Asp38 of bacteriorhodopsin on the electric dipole moments of purple membranes

被引：1
作者：
Tuparev, N [1 ]
Taneva, SG
Lazarova, T
Padros, E
Tóth-Boconádi, R
Petkanchin, IB
机构：
[1] Bulgarian Acad Sci, Inst Biophys, BU-1113 Sofia, Bulgaria
[2] Univ Autonoma Barcelona, Dept Bioquim & Biol Mol, Unitat Biofis, Bellaterra 08193, Barcelona, Spain
[3] Hungarian Acad Sci, Biol Res Ctr, Inst Biophys, H-6701 Szeged, Hungary
[4] Bulgarian Acad Sci, Inst Phys Chem, BU-1113 Sofia, Bulgaria
来源：
COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS | 1999年 / 148卷 / 1-2期
关键词：
bacteriorhodopsin; deionized purple membranes; D38R mutant; electric polarizability; permanent dipole moment;
D O I：
10.1016/S0927-7757(98)00596-2
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
The effect of single amino acid substitution and membrane bound cations on the orientational behavior of purple membrane fragments was studied by electric light scattering. A direct experimental evidence for the contribution of the surface-exposed Asp38 amino acid residue of bacteriorhodopsin to the membrane electric dipole moments is presented. The strong drop of the permanent electric dipole moment upon deionization of wild type bR and D38R mutant indicates the cation binding sites location on the extracellular membrane surface. (C) 1999 Elsevier Science B.V. All rights reserved.
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页码：113 / 119
页数：7
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