John (Jack) T. Simpson SAIC-Frederick Office: 301-846-6702 FAX: 301-846-7269 E-mail: jack@codon.nih.gov Job Title: Scientist Ph.D. in Analytical Chemistry from American University

Speaker: John (Jack) T. Simpson, Protein Chemistry Laboratory, SAIC-Frederick, Frederick, MD 21701

Topic: Affinity Capture Isolation and Characterization of Proteins and Peptides: SPR-MS - Video (running time 00:42:16) ^*

Place: Building 549, Auditorium, NCI at Frederick, Frederick, MD

Time: Tuesday, November 12, 2002, at 2:00 PM

Abstract: The characterization of protein interactions: protein-protein, protein-DNA or protein-ligand, is central to the elucidation of the role of proteins in vivo. A key technique for studying these interactions is surface plasmon resonance (SPR) spectroscopy. Using SPR, kinetic studies can be performed on the binding of analytes to targets bound to a chip surface. While SPR is exquisitely sensitive, the detection of binding partners is non-specific. To address this concern, and to take advantage of the inherent affinity capture abilities of the SPR chips used, several groups have focused on combining SPR with mass spectrometry. The purpose of this discussion will be an introduction to the principles of SPR and recent advances in interfacing SPR with mass spectrometry. In addition, our recent work combining MALDI with SPR for the characterization of HIV nucleocapsid protein (NCp7) will be presented.

____________________

^* Video viewing minimally requires the latest free version of RealPlayer® and a 56 Kbps dial-up bandwidth.