The application by five P.I.'s proposes to use surface plasmon resonance for the kinetic and thermodynamic analysis of specific protein-protein and protein-nucleic acid interactions in a variety of biological systems. The RAJBHANDARY laboratory will perform studies of protein synthesis initiation in eubacteria and in eukaryotes. The molecular mechanisms underlying the specific interaction between the E. coli and human initiator transfer RNAs and the corresponding protein synthesis initiation factors IF2 and eIF2 will be studied using wild type and mutant initiator transfer RNAs. The KHORANA laboratory will study binding and kinetic constants of protein-protein interactions in visual processes (sensitization and desensitization) following light-activation of the vertebrate photoreceptor rhodopsin. Initial focus will be on interactions between activated receptor and the G protein, transducin, on the one hand and between the receptor and rhodopsin kinase on the other. The KIM laboratory will study peptides from the core of HIV gp41, that are known to be inhibitors of HIV infection. The kinetics of association and dissociation of these peptides, and derivatives of these peptides, will be investigated in order to provide information to assist the development of drugs to treat AIDS. The KRIEGER laboratory will study cell surface scavenger receptors which bind chemically modified lipoproteins and have been implicated in atherogenesis, in the recognition and clearance of apoptotic cells and toxic and pathogenic substances, and in HDL metabolism. BIACORE instrument will be used to explore the complex binding properties of these diverse, multiligand receptors. The SAUER laboratory is engaged in studies of (i) repressor- DNA interactions, (ii) how intracellular proteases recognize specific sequences in proteins targeted for destruction and (iii) factors that influence homo versus heterodimerization of the Arc repressor and its variants.
|Mayer, Christine; Kohrer, Caroline; Kenny, Eimear et al. (2003) Anticodon sequence mutants of Escherichia coli initiator tRNA: effects of overproduction of aminoacyl-tRNA synthetases, methionyl-tRNA formyltransferase, and initiation factor 2 on activity in initiation. Biochemistry 42:4787-99|