Abstract:
:We have mapped the interface between the two transmembrane alpha-helices in the membrane domain of the Escherichia coli enzyme leader peptidase by analyzing disulfides formed between pairs of cysteine residues introduced near their respective periplasmic ends. The interface is formed primarily from aliphatic amino acids, and the two helices appear to pack against each other in a left-handed supercoil. We suggest that disulfide mapping may be a generally applicable approach for the construction of models of helix-helix interfaces in membrane proteins.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Whitley P,Nilsson L,von Heijne Gdoi
10.1021/bi00084a020subject
Has Abstractpub_date
1993-08-24 00:00:00pages
8534-9issue
33eissn
0006-2960issn
1520-4995journal_volume
32pub_type
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