As the human genome comes close to being completely identified, attention is turning to protein characterization, because the proteins are the substances actually involved in physiological processes, individually, posttranslationally modified and/or as part of complexes. State-of-the-art protein identification is based on mass spectrometric characterization of proteolytic peptides, either through peptide mapping data or through sequence tag data, combined with data base searching. In addition to protein identification, identification of post-translational modifications and sites of modification are extremely important aspects of protein characterization. Phosphorylation of proteins controls basic cellular processes and determination of the state of phosphorylation of a protein and the specific sites of phosphorylation provides important information that can be used for proposing mechanistic hypotheses, as well as for understanding the processes involved. We are actively developing and applying mass spectrometry-based methods for the characterization of phosphoproteins.

Agency
National Institute of Health (NIH)
Institute
National Institute of Environmental Health Sciences (NIEHS)
Type
Intramural Research (Z01)
Project #
1Z01ES050171-07
Application #
7328433
Study Section
(LSB)
Project Start
Project End
Budget Start
Budget End
Support Year
7
Fiscal Year
2006
Total Cost
Indirect Cost
Name
U.S. National Inst of Environ Hlth Scis
Department
Type
DUNS #
City
State
Country
United States
Zip Code
Terajima, Masahiko; Perdivara, Irina; Sricholpech, Marnisa et al. (2014) Glycosylation and cross-linking in bone type I collagen. J Biol Chem 289:22636-47
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