Robert J. Hohman, Ph.D., ACLAM Diplomate
Protein Chemistry Section
TW1 Room 1004
5640 Fishers Lane
Rockville, MD 20852
The Protein Chemistry Section enables intramural NIAID investigators to use state-of-the-art applications in mass spectrometry, bioinformatics, peptide synthesis and analysis, and protein sequencing in their research programs.
Mass spectrometry provides extensive support in separation, analysis, and characterization and quantitation of peptides and proteins. Our primary work involves bottom-up proteomics using a state-of-the-art high mass accuracy instrument.
Bioinformatics for mass spectrometry performs both label-free and labeled quantitation methods in addition to routine parsimony analysis.
Peptide synthesis and analysis provides synthetic peptides, peptide-carrier protein conjugates, peptide purification, and quality control analyses. In addition, our staff is available for advice and consultations. In cooperation with protein sequencing and mass spectrometry, extensive support is available for expert analysis and characterization of peptides, proteins, and small bio-molecules.
Protein sequencing enables intramural NIAID investigators to use de novo Edman protein sequencing, using ABI Procise protein sequencers. We offer N-terminal sequence analyses that provide direct chemical sequences for quality control of known proteins or identification of proteins not presently in any database.
Dr. Hohman received his Ph.D. in microbiology from NIH and the University of Maryland in 1982. After a three-year postdoctoral position in the laboratory of biochemistry at the Pasteur Institute in Paris, he returned to NIH for a second postdoctoral appointment. In 1992, he joined Oncor Inc., a biotechnology company that specialized in DNA diagnostics, and became the vice president of research and development. In 2000, he was recruited back to NIH to become the DIR associate director for research technologies and chief of the Research Technologies Branch.
This page was last updated on August 3rd, 2017