Prof. Jarrod Marto

MoSE 3201A
Thursday, October 31, 2013 - 11:00am to 12:00pm

Why All Proteins Expressed by a Genome Should be Identified and How to do it

Next-generation DNA sequencing has greatly expanded our understanding of the genomic landscape associated with normal physiology and human disease. These studies have effectively re-kindled interest in experiments designed to discover novel biomolecules and simultaneously quantify their activities in metabolic, signaling, or other biological pathways. Establishing a parallel trajectory for this paradigm in genome-scale protein interrogation is complicated by the wide dynamic range of protein expression, diverse repertoire and stoichiometry of protein post-translational modifications, as well as fundamental limitations in the technologies used to survey the proteome. Despite these hurdles, the functional content of protein-level data represents an important complement to genomic-based studies. Here I will review the challenges and opportunities associated with comprehensive proteome characterization, and describe our efforts to develop an automated deep efficient peptide sequencing and quantification (DEEP SEQ) mass spectrometry platform that provides unprecedented separation capacity, rapid sequencing speed, and quantification of proteins across the entire range of mammalian gene expression and protein translation.

Contact Information: 

Prof. Facundo Fernandez (404-385-4432).

Map of Georgia Tech

School of Chemistry & Biochemistry

901 Atlantic Drive Atlanta, GA 30332-0400

(404) 894-4002 (phone) | (404) 894-7452 (fax)