Abstract
Mass spectrometry-based protein identification protocols have propelled proteomics to the forefront of biomedical research.  Provided with available genomic and/or protein sequence information in databases, protein identification by peptide mass mapping and peptide sequencing by MS fragmentation is efficient.  However, in situations in which sufficient genome and protein sequence data is unavailable, mass spectrometric methods can be used for de novo protein sequencing.  The mass measurement accuracy of MS provides a unique capability to generate peptide sequence.  Top-down sequencing of intact proteins provides alignment of peptide sequences derived from the bottom-up approach.

Moreover, the structural determination of proteins and protein complexes plays an important role in the fundamental understanding of biochemical pathways.  Proteins serve to interact with other biochemical entities, for example, with smaller molecular species such as metal ions, nucleotide cofactors or with other proteins.  The study of weakly-bound, protein noncovalent complexes by electrospray ionization MS has provided structural biologists and biochemists a sensitive and accurate means to determine assembly size and binding partner stoichiometry for a number of important complexes.  New methods based on electrospray ionization and ion mobility measurements allow for characterization of protein complexes in excess of 10 MDa in size.

Background
Joe Loo is Professor of Biochemistry and Biological Chemistry at the University of California-Los Angeles and the Director of the UCLA Mass Spectrometry and Proteomics Technology Center.  Previously, he was Biological Mass Spectrometry Group Leader at Pfizer Global Research and Development (formerly Parke-Davis Pharmaceutical Research) in Ann Arbor, MI.  His research interests include the development of novel bioanalytical methods for the structural characterization of proteins and their post-translational modifications, proteomics and its application for biomedical research, and the development and application of mass spectrometry for the study of noncovalently-bound macromolecular complexes and their interactions with ligands.  He has been an Editorial Board member for Journal of the American Society for Mass Spectrometry, Analytical Chemistry (A-page), and Bioconjugate Chemistry.  He was a Member-at-Large on the American Society for Mass Spectrometry Board of Directors.  Currently, he serves on the NIH BECM (Bioanalytical Engineering and Chemistry) Study Section.  Joe received his B.S. degree in Chemistry from Clarkson University and his Ph.D. in Analytical Chemistry from Cornell University with Professor Fred W. McLafferty.  He did his postdoctoral research at Battelle-Pacific Northwest National Laboratory with Dr. Richard D. Smith.

Meeting details

Date:	Tuesday	August 27, 2002
Time:	6:00 pm	Social hour, registration (no-host cocktails)
	7:00 pm	Dinner
	8:00 pm	Lecture
Dinner:	Choice of:	Chicken
		Pasta
	includes	(various side dishes & dessert)
Cost:	$25.00	BAMS members.  Reservations required by noon on Friday August 23, 2002
	$35.00	Non-members.  Reservations required by noon on Friday August 23, 2002
	$15.00	Students only.  Reservations required by noon on Friday August 23, 2002

Note: 2002 dues need to be paid to obtain member price.  Dues ($20) may be paid while registering for dinner.

Maps & directions
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1221 Chess Drive
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The San Francisco Bay Area Mass Spectrometry discussion group was formed in 1980 to provide a regular gathering for people interested in mass spectrometry and allied topics. BAMS currently has a membership of about 280 individual and 20 corporate members, and meets 8-10 times per year for a midweek dinner and lecture.  Meetings attract between 30 and 90 people, and are held at a restaurant or hotel in the bay area convenient for our speaker.  We usually convene at 6:00 pm for cocktails, dinner at 7:00 pm, and lecture at 8:15 pm.

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Last update: 8/14/02.