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Specificity and promiscuity in membrane helix interactions
Author(s) -
Lemmon Mark A.,
Engelman Donald M.
Publication year - 1994
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(94)00467-6
Subject(s) - promiscuity , transmembrane domain , folding (dsp implementation) , transmembrane protein , membrane protein , helix (gastropod) , integral membrane protein , chemistry , biophysics , lipid bilayer , function (biology) , membrane , biochemistry , biology , microbiology and biotechnology , receptor , ecology , snail , electrical engineering , engineering
Transmembrane α‐helices can associate with one another in lipid bilayers. This association is important in the folding and oligomerization of many integral membrane proteins, and may also play a role in their function. The interactions between helices may be highly specific or relatively non‐specific, and their roles may differ accordingly. These two cases are discussed.