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The leader peptides from bacteriorhodopsin and halorhodopsin are potential membrane‐spanning amphipathic helices
Author(s) -
von Heijne Gunnar,
Segrest Jere P.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81497-7
Subject(s) - bacteriorhodopsin , halorhodopsin , amphiphile , chemistry , membrane , biophysics , halobacteriaceae , membrane protein , biochemistry , crystallography , biology , organic chemistry , halobacterium salinarum , copolymer , polymer
We show that the N‐terminal leader peptides from the bacterial membrane proteins bacteriorhodopsin and halorhodopsin can be expected to form amphipathic α‐helices with a highly hydrophobic nonpolar face and a narrow, negatively charged polar face. This finding is discussed in terms of a model for the integration of these proteins into the bacterial membrane.