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Conformational changes of a mitochondrial precursor protein on binding to phospholipid vesicles and SDS micelles A circular dichroism and fluorescence spectroscopy study
Author(s) -
Endo Toshiya,
Oya Masanao
Publication year - 1989
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(89)80618-0
Subject(s) - circular dichroism , cardiolipin , chemistry , micelle , vesicle , phospholipid , conformational change , fluorescence spectroscopy , biophysics , fluorescence , biochemistry , biology , membrane , organic chemistry , physics , quantum mechanics , aqueous solution
Conformations of an artificial mitochondrial precursor protein pCox IV‐DHFR have been analyzed by CD and fluorescence spectroscopy in the presence of (cardiolipin‐rich) phospholipid vesicles or SDS micelles. Binding of pCox IV‐DHFR to phospholipid vesicles involves a conformational change, which is presequence‐dependent, accompanies alteration in the secondary structure of the DHFR moiety, but is different from total unfolding of the polypeptide chain. On the other hand, a conformational change of the fusion protein on binding to the micelles of a positively charged detergent, SDS, is not presequence‐dependent.