Ryuji Kobayashi, Ph.D.
1990, Nagasaki University
UT M. D. Anderson Cancer Center
Molecular Pathology
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Ryuji Kobayashi, Ph.D. 1990, Nagasaki University UT M. D. Anderson Cancer Center |
Research Interests: method development for proteomics research; Protein S-nitrosylation
Proteomics is now in its second decade. Completion of genome project and development of mass spectrometry-based technology has driven the field of proteomics research. It had been hoped that there would be dramatic understanding of biology and discovery of biomarkers. Unfortunately, proteins are present in large dynamic range of concentrations that exceed the range of standard methods of mass spectrometry or in many forms following multiple modifications. In addition, mass spectrometry lacks selectivity and detects more abundant proteins first. Thus recent proteomic studies have faced the major obstacles of dynamic range of concentration, complexity and interference of abundant proteins.
I invented a unique isolation method of the blocked N-terminal peptide of protein which is post-translationally modified. I am interested in applying this method for three kinds of proteomic studies: cellular proteomics, plasma protein biomarker search, and study of noncanonical initiation of translation products.
Another research interest is to study mechanism of protein S-nitrosylation. S-nitrosylation of protein may have a critical role in regulation of protein function. S-nitrosylation of proteins occurs at the site that contains a motif of -D/E-C-R/K- or -R/K-C-D/E-. However, the mechanism of protein S-nitrosylation is not well understood. We are searching enzymes which nitrosylate/denitrosylate protein.
A tutorial in my laboratory would provide experience with basic protein chemistry techniques, mass spectrometry analysis of protein, purification and biochemical characterization of protein.
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Koomen JM, Zhao H, Li D, Nasser W, Hawke DH, Abbruzzese JL, Baggerly KA, Kobayashi R (2005) Diagnostic protein discovery using liquid chromatography-mass spectrometry for proteolytic peptide targeting. Rapid Commun Mass Spectrom. 19, 1624-1636.
Koomen JM, Li D, Xiao L, Liu TC, Coombes KR, Abbruzzese JL, Kobayashi R (2005) Direct tandem mass spectrometry reveals limitations in protein profiling experiments for plasma biomarker discovery. J Proteome Res. 4, 972-981.
Coussot G, Hawke DH, Mularz A, Koomen JM, Kobayashi R (2007) A method for the isolation of blocked N-terminal peptides. Anal Biochem, 361, 302-304.
Program Affiliation:
Program in Molecular Pathology