ORGN 216 |
| Genetic mutations in the transmembrane (TM) domains of proteins underlie the causes of many human diseases, including several forms of cancer, diabetes, and cystic fibrosis. Our research goals are to determine in a systematic manner how amino acid sequence motifs and packing interactions between membrane-spanning helices confer the biologically functional structures of proteins within membranes – and to determine the molecular basis for dysfunction in disease-causing mutants. The method of Lys-tagging has been developed to facilitate synthesis and biophysical analysis of the required highly hydrophobic TM peptides. The lecture will focus on evaluating the determinants of helix-helix packing and assembly in (i) single-spanning TM peptides that form parallel homo-dimers with varying affinities; (ii) TM helix peptides with two interactive faces that mediate oligomerization in small multidrug resistance proteins; and (iii) de novo designed hydrophobic TM peptide-loop-TM peptide constructs that form anti-parallel helical hairpin structures. |
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Ralph F. Hirschmann Award in Peptide Chemistry
1:30 PM-5:00 PM, Monday, 27 March 2006 Georgia World Congress Center -- C303/304/305, Oral
Division of Organic Chemistry |