Membrane proteins play a very important role in many cellular processes, and account for 20-40% of the products of open reading frames of known genomes. Their association with a number of diseases [1,2] has stimulated great interest in these proteins, in particular, in understanding how they function in their native lipid environments.
Because membrane proteins are embedded in a lipid matrix, the application of routine structure determination methods, namely solution state nuclear magnetic resonance (NMR) and x-ray crystallography, is precluded. The limited number of structures of membrane proteins reported to date is evidence of the difficulty in applying these methods to such systems [3,4]. In recent years, developments in the field of solid state NMR have led to an emergence of biomolecular studies using this technique. One significant advantage of using solid state NMR to study membrane proteins is that these can be studied in native-like phospholipid environments directly . A further advantage of solid state NMR is that it also allows the study of membrane protein/peptide dynamics. Information on peptide mobility can provide insight into the conformational rearrangements which are linked to the peptide's biologal activity in the membrane.
Research in my laboratory focuses on the application and development of solid state NMR methods to characterise the structure and dynamics of membrane proteins. To gain insight into membrane peptide/protein, a number of relevant systems will be studied. Specifically, studies on membrane protein/lipid and membrane protein/ligand interactions will be undertaken.
1. B.W. Morrison, J. Moorman, G. Kowdley, Y. Kobayashi, L. Jones, P. Leder, MAT-8, a novel phospholemman-like protein expressed in human breast-tumors, induces a chloride conductance in Xenopus oocytes, J. Biol. Chem., 270, 2176 (1995).
2. K. Strebel, T. Klimkait, M. A. Martin, A novel gene of HIV-1, Vpu, and its 16-kilodalton product, Science, 241, 1221 (1988).
3. M. Hartmut, Crystallization of Membrane Proteins, CRC Press, Boston, MA (1991).
4. C.H.M. Papavoine, B. Christiaans, R. Folmer, R. Konings, C.W. Hilbers, Solution structure of the M13 major coat protein in detergent micelles , J. Mol. Biol., 282, 401 (1998).
5. A.Watts, Solid-state NMR approaches for studying the interaction of peptides and proteins, Biochim. Biophys. Acta, 1376, 297 (1998).