Al Burlingame, PhD

Phone: +1 415 476-5641
Fax: +1 415 502-1655

600 16th St, Rm N472H
UCSF Box 2240
San Francisco, CA 94158
United States

Educational programs

PhD Program in Chemistry and Chemical Biology (CCB)

UCSF centers, institutes, and research programs

What I do

My research interests focus on the development of state of the art methodologies in mass spectrometry for use in advancing our global knowledge of human biology, specifically the dynamic, epigenetic modulation and regulation of the proteome.

Research area

My research expertise

Bioanalytical chemistry, Mass spectrometry

Degrees

PhD, Chemistry/Physics, Massachusetts Institute of Technology (MIT), 1962
BS, Chemistry, University of Rhode Island, 1959

Biography

My group has long-standing, extensive expertise and experience in mass spectrometry, proteomics and systems biology, especially focused on sequencing, identification and study of unknown proteins, and the detection, assignment and site-specific dynamics of posttranslational modifications of proteins, particularly OGlcNAcylation, phosphorylation, acetylation, methylation and ubiquitinylation. Over many years we have collaborated with the neurobiological community extensively, including structural characterization of the GPI membrane anchor of the prion protein, structure of the lysyl oxidase co-factor, identification and PTM regulation of proteins in the retrograde signaling complexes in damaged axons, the O-GlcNAc/phosphorylation dynamics at the murine synapse, identification of new proteins involved in the Nodes of Ranvier, etc.

In addition to the work in proteomics and epigenetics above, we have focused significant effort on other studies concerning the architecture of protein complexes and machines for which angstrom resolution structural information has not yet been tractable. For example we have developed a new lysine-lysine cross-linking strategy based on chemical reductive amination that provides comprehensive sequence and cross-link site assignments using electron transfer dissociation (ETD). This information provides accurate distance constraints that complement cryoEM and computer modeling efforts. In parallel software algorithms and scoring strategies have been developed that greatly facilitates the assignment of cross-linked peptides in general. Very recently we have initiated a thrust into development and application of methodology to measure protein complexes directly in the gas phase using a newly acquired high mass Orbitrap Exactive instrument (m/z < 22,000). This effort will complement our long-standing work on chemical cross-linking of protein complexes and machines.

Finally, we have developed a general suite of programs and software tools required for processing large scale mass spectral data sets (HCD, ETD, etc) and stable isotopic labeling experiments (SILAC, iTRAQ, etc) called Protein Prospector.