Abstract：
:The topology of E. coli inner membrane proteins depends primarily on the distribution of positively charged residues in the molecule. We have constructed model proteins with four potential transmembrane stretches and have systematically explored the topological effects of lysines placed in the loops connecting the transmembrane spans. Our results indicate that membrane insertion is locally determined, with individual "helical hairpins" inserting independently of each other. Topologically "frustrated" molecules, where the charge distribution is such that different parts of the molecule would prefer to insert with incompatible orientations, adopt "leave-one-out" topologies in which only 3 of the 4 potential transmembrane stretches span the membrane. These results are relevant for our general understanding of both membrane protein biogenesis and the evolution of multi-spanning membrane proteins.
journal_name
Celljournal_title
Cellauthors
Gafvelin G,von Heijne Gdoi
10.1016/0092-8674(94)90155-4subject
Has Abstractpub_date
1994-05-06 00:00:00pages
401-12issue
3eissn
0092-8674issn
1097-4172pii
0092-8674(94)90155-4journal_volume
77pub_type
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