BLUE FORM OF BACTERIORHODOPSIN AND ITS ORDER-DISORDER TRANSITION DURING DEHYDRATION

Citation
S. Wakatsuki et al., BLUE FORM OF BACTERIORHODOPSIN AND ITS ORDER-DISORDER TRANSITION DURING DEHYDRATION, Biochimica et biophysica acta. Bioenergetics, 1185(2), 1994, pp. 160-166
Citations number
37
Categorie Soggetti
Biology,Biophysics
ISSN journal
00052728
Volume
1185
Issue
2
Year of publication
1994
Pages
160 - 166
Database
ISI
SICI code
0005-2728(1994)1185:2<160:BFOBAI>2.0.ZU;2-2
Abstract
Freshly-prepared blue membranes from Halobacterium halobium, previousl y reported to be disordered, are shown to have a distinct crystal latt ice structure, slightly different from the native form. The lattice of the blue form is disrupted irreversibly when dehydrated. The disorder process was observed using time-resolved small-angle X-ray diffractio n and analyzed by radial autocorrelation functions. The diffraction pe aks of the in-plane lattice first sharpen and increase due to improved membrane orientation, then the trimer lattice becomes disordered and the unit cell dimension decreases by 1.8 Angstrom. In contrast, dehydr ation of purple membranes does not disorder the lattice, and the unit cell dimension shrinks by only 1.0 Angstrom. Comparisons of radial aut ocorrelation functions for the blue membrane during drying show drasti c loss of inter-trimer, long-range correlation while the intra-trimer, short-range correlations remain more or less unchanged. This suggests that the deionized protein trimers can maintain their overall structu re during the dehydration, even though the lattice dimension decreases appreciably and the two-dimensional crystallinity is disrupted.