Secondary Structure and Topology of a Mitochondrial Presequence Peptide Associated with Negatively Charged Micelles. A 2D 1H-NMR Study

Autor:	Johanna M. Leenhouts, Vladimir Chupin, Ben de Kruijff, and Anton I. P. M. de Kroon
Rok vydání:	1996
Předmět:	Phosphatidylglycerol chemistry.chemical_classification Circular dichroism Chemical shift Peptide Topology Biochemistry Micelle chemistry.chemical_compound Crystallography chemistry Helix Proton NMR Protein secondary structure
Zdroj:	Biochemistry. 35:3141-3146
ISSN:	1520-4995 0006-2960
Popis:	In this study the secondary structure and topology of the peptide, corresponding to the presequence of cytochrome oxidase subunit IV (p25) in a negatively charged membrane-mimetic environment, were assessed by circular dichroism and two-dimensional nuclear magnetic resonance. The micelles used consisted of dodecylphosphoglycol (DPG), a mild anionic detergent with a headgroup resembling that of phosphatidylglycerol. The secondary structure was analyzed by interresidue nuclear Overhauser enhancement measurements and chemical shifts of backbone protons. The data revealed alpha-helix formation of the peptide upon interaction with the micelles, both in the N- and in the C-terminal halves, which are separated from each other by the proline residue at position 13. The topology of the peptide was studied by determining the effect of spin-labeled 12-doxylstearate on the line widths of the peptide proton resonances. This method revealed the insertion of hydrophobic residues of both the N- and the C-terminal halves of p25 into the hydrophobic environment of the micelles, demonstrating the orientation of the amphiphilic helix.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::06b97940a3c2bf25c6a06001df07438d https://doi.org/10.1021/bi952482a Zobrazit plný text záznamu