~1H- and ~2H-NMR studies of a fragment of PMP1, a regulatory subunit associated with the yeast plasma membrane H~+ -ATPase. Conformational properties and lipid-peptide interactions

摘要

PMP1 is a 38-residue polypeptide associated with the yeast plasma membrane H~+ -ATPase, found to regulate the enzyme activity. To investigate the molecular basis of the PMP1 biological function, the conformational properties of a synthetic PMP1 fragment, A18-F38, Comprising the predicted C-terminal cytoplasmic domain and a part of the transmembrane anchor have been studied by ~1H- and ~2H-NMR Spectroscopies. High resolution ~H-NMR experiments showed that, in deuterated DPC micelles, the A18-G34 segment adopts a well defined Helix conformation.