Cardiolipin modulates the secondary structure of the presequence peptide of cytochrome oxidase subunit IV: a 2D 1H-NMR study
| Autor: | Anton I.P.M. de Kroon, Johanna M. Leenhouts, Vladimir Chupin, Ben de Kruijff |
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| Rok vydání: | 1995 |
| Předmět: |
Models
Molecular Circular dichroism Magnetic Resonance Spectroscopy Stereochemistry Cardiolipins Protein subunit Phosphorylcholine Molecular Sequence Data Biophysics Peptide Protein Sorting Signals Conformational flexibility Biochemistry Mitochondria Heart Protein Structure Secondary Electron Transport Complex IV chemistry.chemical_compound Structural Biology Genetics Cardiolipin Cytochrome c oxidase 2D NMR Amino Acid Sequence Mitochondrial presequence Molecular Biology Protein secondary structure Micelles chemistry.chemical_classification Enzyme Precursors biology Circular Dichroism Cell Biology chemistry Liposomes biology.protein Proton NMR Lipid-protein interaction Two-dimensional nuclear magnetic resonance spectroscopy Micelle |
| Zdroj: | FEBS letters. 373(3) |
| ISSN: | 0014-5793 |
| Popis: | 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, alpha-helix formation was observed. The alpha-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 alpha-helical conformation of p25, modulated by CL. |
| Databáze: | OpenAIRE |
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