Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane

Bacteriorhodopsin is the one of the best-studied models of an ion pump. Five atomic models are now available, yet their comparison reveals differences of some loops connecting the seven transmembrane alpha-helices. In an attempt to resolve this enigma, topographs were recorded in aqueous solution wi...

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Bibliographic Details
Published inJournal of molecular biology Vol. 285; no. 5; pp. 1903 - 1909
Main Authors Müller, D J, Sass, H J, Müller, S A, Büldt, G, Engel, A
Format Journal Article
LanguageEnglish
Published England 05.02.1999
Subjects
Bacteriorhodopsins - chemistry
Bacteriorhodopsins - metabolism
Buffers
Crystallization
Cytoplasm - chemistry
Cytoplasm - metabolism
Microscopy, Atomic Force - methods
Models, Molecular
Protein Conformation
Purple Membrane - chemistry
Purple Membrane - metabolism
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Summary:Bacteriorhodopsin is the one of the best-studied models of an ion pump. Five atomic models are now available, yet their comparison reveals differences of some loops connecting the seven transmembrane alpha-helices. In an attempt to resolve this enigma, topographs were recorded in aqueous solution with the atomic force microscope (AFM) to reveal the most native surface structure of bacteriorhodopsin molecules in the purple membrane. Individual peptide loops were observed with a lateral resolution of between 4.5 A and 5.8 A, and a vertical resolution of about 1 A. The AFM images demonstrate for the first time, that the shape, the position, and the flexibility of individual polypeptide loops depend on the packing arrangement of bacteriorhodopsin molecules in the lipid bilayer.
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ISSN:0022-2836
DOI:10.1006/jmbi.1998.2441