Cardiolipin modulates the secondary structure of the presequence peptide of cytochrome oxidase subunit IV: a 2D 1H‐NMR study

FEBS Letters

de Kroon, Anton I.P.M.¹  Chupin, Vladimir¹  Leenhouts, Johanna M.¹  de Kruijff, Ben¹ 

[1] Department of Biochemistry of Membranes, Center for Biomembranes and Lipid Enzymology, Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands

关键词: Mitochondrial presequence;    2D NMR;    Micelle;    Cardiolipin;    Conformational flexibility;    Lipid-protein interaction;    CD;    circular dichroism;    CL;    cardiolipin;    2D;    two-dimensional;    3D;    three-dimensional;    DPC;    dodecylphosphocholine;    DPC-d38;    [2H38]dodecylphosphocholine;    NMR;    nuclear magnetic resonance;    NOE;    nuclear Overhauser enhancement;    NOESY;    2D nuclear Overhauser enhancement spectroscopy;    p25;    peptide corresponding to the presequence of cytochrome oxidase subunit IV;    PC;    phosphatidylcholine;    TOCSY;    2D total correlation spectroscopy;    TPPI;    time-proportional phase increment;   

DOI  :  10.1016/0014-5793(95)01054-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 proline¹³ 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.

【 授权许可】

Unknown