Vpu is a small (81 residue) membrane protein encoded in the genome of HPV-I. Because of its small size and integral function in the HIV-1 lifecycle, NMR structural studies of Vpu can contribute to the development of membrane protein structure elucidation methods while simultaneously pursuing answers to AIDS-related research questions. The focus of this study is to develop NMR methods for determining the structures of membrane proteins. Specifically, the goals are to: 1. Determine the structure of the membrane protein Vpu; and 2. Utilize the structural information to describe its biological functions. Solid-state NMR spectroscopy will be performed on oriented lipid bilayer samples of Vpu. These studies will be compared to those obtained from complementary techniques, including solution-state NMR on micelle samples and solid-state MAS NMR on unoriented bilayer samples.
| Park, Sang Ho; Mrse, Anthony A; Nevzorov, Alexander A et al. (2006) Rotational diffusion of membrane proteins in aligned phospholipid bilayers by solid-state NMR spectroscopy. J Magn Reson 178:162-5 |
| De Angelis, Anna A; Nevzorov, Alexander A; Park, Sang Ho et al. (2004) High-resolution NMR spectroscopy of membrane proteins in aligned bicelles. J Am Chem Soc 126:15340-1 |
