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Secondary structure of a mitochondrial signal peptide in lipid bilayer membranes
Author(s) -
Tamm Lukas K.,
Bartoldus Ingrid
Publication year - 1990
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(90)80441-k
Subject(s) - cardiolipin , phosphatidylglycerol , chemistry , liposome , phosphatidylcholine , circular dichroism , lipid bilayer , cytochrome c oxidase , helix (gastropod) , biophysics , protein secondary structure , membrane , biochemistry , crystallography , phospholipid , mitochondrion , biology , ecology , snail
The secondary structure of the synthetic signal peptide of cytochrome c oxidase subunit IV (coxIV‐25) has been measured by circular dichroism spectroscopy in different lipid environments. CoxIV‐25 is polymorphic in membranes. It forms an amphiphilic α‐helix both in negatively charged lipid bilayers (up to 49% helix) and in detergent micelles (up to 42% helix). In associaton with bilayers of the zwitterionic lipid phosphatidylcholine, coxIV‐25 takes an aperiodic, unidentified structure. CoxIV‐25 is also partially α‐helical in bilayers of cardiolipin, mitochondrial lipid extracts and mixtures of synthetic phosphatidylcholine and phosphatidylglycerol.