13C-13C correlation spectroscopy of membrane-associated influenza virus fusion peptide strongly supports a helix-turn-helix motif and two turn conformations.

ABSTRACT: The influenza virus fusion peptide (IFP) is the N-terminal domain of the viral hemagglutinin protein, binds to the endosomal membrane, and plays a critical role in fusion between the viral and endosomal membranes which is a primary step in infection. The IFP is also an important system for testing simulation methods for membrane-associated peptides. In detergent, the IFP forms helix-turn-helix and helix-turn-strand structures at pH 5.0 and 7.4, respectively, while simulations in membranes by different groups have yielded conflicting results with some reports of a continuous helix without a turn. In this study, (13)C-(13)C NMR correlation spectra were obtained for the membrane-associated IFP and the (13)C chemical shifts supported a helix-turn-helix motif at both pH 5.0 and 7.4 with an alte

SUBMITTER: Sun Y 

PROVIDER: S-EPMC2772195 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature