In collaboration with M. Montal, UCSD, we have been investigating peptides with sequences corresponding the helical regions of large membrane embedded receptors, including the acetylcholine receptor, glycine receptor, and the NMDA receptor. The research on the NMDA Receptor is also in collaboration with M. Maccecchini of Symphony Pharmaceuticals. 20-25 residue peptides corresponding to the M2 segment apparently aggregate in membranes so that they function as channels. We have synthesized and expressed these peptides, and labeled them with stable isotopes, for NMR studies. The solid-state NMR studies show the trans-membrane orientation of the helices of these peptides. The uniformly labeled peptides in oriented bilayers are among the first targets for the multidimensional experiments we are developing for both increasing spectroscopic resolution and structure determination.
| Valentine, Kathleen G; Mesleh, Michael F; Opella, Stanley J et al. (2003) Structure, topology, and dynamics of myristoylated recoverin bound to phospholipid bilayers. Biochemistry 42:6333-40 |
| Montal, M; Opella, S J (2002) The structure of the M2 channel-lining segment from the nicotinic acetylcholine receptor. Biochim Biophys Acta 1565:287-93 |
| Opella, Stanley J; DeSilva, Tara M; Veglia, Gianluigi (2002) Structural biology of metal-binding sequences. Curr Opin Chem Biol 6:217-23 |
| Jiang, F; Gorin, A; Hu, W et al. (1999) Anchoring an extended HTLV-1 Rex peptide within an RNA major groove containing junctional base triples. Structure 7:1461-72 |
| Marassi, F M; Ma, C; Gratkowski, H et al. (1999) Correlation of the structural and functional domains in the membrane protein Vpu from HIV-1. Proc Natl Acad Sci U S A 96:14336-41 |
