Skip Navigation

Research Technologies Branch

Skip Content Marketing
  • Share this:
  • submit to facebook
  • Tweet it
  • submit to reddit
  • submit to StumbleUpon
  • submit to Google +

Robert J. Hohman, Ph.D.

Photo of Robert J. Hohman, Ph.D. 

Chief, Research Technologies Branch
Chief, Protein Chemistry Section, RTB

Major Areas of Expertise

  • Edman (N-terminal) protein sequencing
  • Peptide synthesis
  • Analytical mass spectrometry (MS)
  • Protein identification
  • Protein separation
  • Assay development
  • Proteomics
  • Bioinformatics
 

Program Description

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.

Instrumentation

Our facility is equipped with specialized instrumentation devoted to the science of protein chemistry, which requires answering biologically relevant questions by examining the structure of proteins at the molecular level.

Mass Spectrometry

  • Electrospray (ES) mass spectrometer (MS) system (API 365 TQMS)
  • AB voyager RP matrix-assisted laser desorption ionization (MALDI) - time of flight MS
  • Micromass electrospray quadropole-orthogonal time of flight (Q-TOF2) MS
  • AB QSTAR XL Hyrbid Q-TOF LC/MS/MS System

Peptide Synthesis

  • Applied Biosystems Model 433A Automated Peptide Synthesizer (with maximum synthetic capability of 0.25mM)
  • Applied Biosystems Voyager RP MALDI-TOF Mass Spectrometer
  • Beckman System Gold Analytical HPLC System with Diode Array Detector
  • Shimadzu VP series HPLC System
  • Waters Model 510 Preparative HPLC System
  • VirTis FREEZEMOBILE 12XL Lyophilizer

Protein Sequencing

  • Applied Biosystems 494clc procise protein sequencer (2) with four cartridge capability
  • Applied Biosystems 494 ht protein sequencer with four cartridge capability
  • Applied Biosystems 173a microblotter capillary lc system
back to top

Research Group

Carl H. Hammer, Ph.D.
Glenn Nardone, Ph.D.
Jan Lukszo, Ph.D.
L. Renee Olano, Ph.D
Mark K. Garfield, M.S.
Ming Zhao, Ph.D.
Raynaldo Martin, B.S.

Specialties

Carl H. Hammer, Ph.D., Mass Spectrometry
L. Renee Olano, Ph.D., Bioinformatics
Jan Lukszo, Ph.D., Peptide Synthesis and Analysis
Mark K. Garfield, M.S., Protein Sequencing
Glenn Nardone, Ph.D., Assay Development
Ming Zhao, Ph.D., Protein Separation

Last Updated October 31, 2012

Last Reviewed October 31, 2012