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Cardiolipin modulates the secondary structure of the presequence peptide of cytochrome oxidase subunit IV: a 2D 1 H‐NMR study
Author(s) -
Chupin Vladimir,
Leenhouts Johanna M.,
de Kroon Anton I.P.M.,
de Kruijff Ben
Publication year - 1995
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(95)01054-i
Subject(s) - chemistry , cardiolipin , circular dichroism , helix (gastropod) , cytochrome c oxidase , protein subunit , protein secondary structure , micelle , stereochemistry , thermostability , n terminus , nuclear magnetic resonance spectroscopy , crystallography , biophysics , biochemistry , peptide sequence , mitochondrion , enzyme , phospholipid , biology , ecology , membrane , snail , gene , aqueous solution
The secondary structure of the presequence of cytochrome oxidase subunit IV (p25) was studied by circular dichroism and 2D nuclear magnetic resonance in micelles of dodecylphosphocholine (DPC) and mixed micelles of DPC and mitochondrial cardiolipin (CL). In both systems, α‐helix formation was observed. The α‐helix stretches from the N‐ to the C‐terminus with a break at the proline residue at position 13. Upon introduction of CL in the DPC micellar system, an increased stability of the helix was observed around proline 13 and in the C‐terminal half. This observation, together with reported results on specific interactions between CL and p25, led to the proposal of a two‐state equilibrium of the α‐helical conformation of p25, modulated by CL.