The MU Proteomics Center is named for Charles W. Gehrke, emeritus professor of Biochemistry, University of Missouri-Columbia. Dr Gerhke joined MU in 1949 and progressed to the rank of full professor. His interest in analytical chemistry and mass spectrometry was one of the factors in naming the Center for Dr Gehrke; benefactors are Lowell and Marian Miller. Read a biographical sketch in celebration of his 85th Birthday (in 2002) here.

The staff of the Charles W. Gehrke Proteomics Center was saddened to hear of Dr. Gehrke’s death Tuesday Feb10th 2009. Professor Gehrke was a pioneer in chromatography and analytical biochemistry.

When the Center first moved to the Bond Life Sciences Center, Dr. Gehrke was a regular visitor to the core and was genuinely interested in our work. He was impressed by our facilities and staff. He sometimes just dropped by, accompanied by friends, and would give a tour of the Center himself. We believe, therefore, he was honored and proud to have official recognition of his service to campus and to the field of chromatography in the form of the named core facility. There was a great turn-out for the naming ceremony in 2004. He kindly organized a lunar sample display for the opening of the Life Sciences Center, on loan from NASA’s Johnson Space Center in Houston, as well as the gas chromatograph he used for his analysis work. Although we have not been graced with a visit in recent years, we will always remember his good natured tone and fervent interest in science.
Dr. Gehrke was never one to rest and as recently as Nov/Dec of 2008 he was working on organizing a NASA/MO symposium, to be held in 2009.

A nice story of Dr. Gehrke’s life, along with service details, was published in 2/11/09’s Columbia Missourian and can be found at: http://www.columbiamissourian.com/stories/2009/02/11/charles-gehrke-researcher-and-businessman-dies-91/

The Proteomics Center provides advanced technologies in protein separation and mass spectrometry identification for researchers at the University of Missouri-Columbia.

Location
Funding
Initiating a project
Fees
Services

Location
The Proteomics Center is located in rooms 212, 213, 213b, and 214 of the Life Sciences Center (1201 E. Rollins Street) on the University of Missouri-Columbia campus. Get directions.

Funding
The Proteomics Center was established by a $1,000,000 equipment grant from Monsanto, Inc. (St. Louis, MO). The Molecular Biology Program, Life Sciences Mission Enhancement, the College of Arts and Sciences, the Division of Biological Sciences, the Department of Chemistry, the Department of Biochemistry, the Interdisciplinary Plant Group, and the Animal Reproductive Cluster have also contributed funds to the development of the Proteomics Center.

Initiating a project
Any project initiated by the Proteomics Center requires a preliminary consultation with Dr. Brian Mooney, Associate Director, to discuss the goal(s) of the project. Consultations are free of charge and can be in the form of an office visit, phone call, or e-mail correspondence. A brief discussion of the project before it is initiated is frequently necessary to clarify the capabilities and limitations of the facility or the technology. After an initial consultation a submission form must be filled out for the service(s) requested. Sample(s) and submission forms(s) must be delivered to the Proteomics Center.

Fees
Fee schedules have been determined based upon consumable, labor, and service contract costs. Fees are negotiable for large projects and for experienced users capable of using instrumentation without guidance. Any fee discount must be discussed with the Associate Director prior to initiation of the project. Under no circumstances are fee schedules to be negotiated with the staff.

Services

• Two-dimensional electrophoresis
  The Proteomics Center is equipped to perform high resolution two-dimensional gel electrophoresis using the Amersham IPGphor or Bio-Rad Protean IEF units and Ettan DALT II systems. The Proteomics Center will perform two-dimensional electrophoresis on any non-hazardous biological samples provided by clients. For highest probability of success samples should be free of salts and prepared as dry precipitates (minimum of 0.1 mg protein) for direct resuspension in isoelectric focusing media. However, the Center will accept whole cell or tissue samples and prepare them for isoelectric focusing either by direct solubilization in IEF media or by an alternative extraction protocol developed by the Proteomics Center. It should be emphasized that multiple samples should be prepared in the same manner if comparisons among the gels are being made.
  

• Image analysis
  The Center is capable of capturing images of Coomassie, silver, or fluorescent stained gels in a 16-bit TIFF format. Currently gels can be analyzed in-house using Phoretix 2D advanced image analysis software. Additionally, the Center has a copy of the DeCyder program for analysis of DIGE (Cydye labelled) gels.

• In-gel digestion of proteins for mass spectrometry
  The Center will prepare tryptic peptide extracts from acrylamide gel sample(s) excised on-site or brought in by the client. Non-trypsin protease digestion can also be performed but must be discussed in advance with the Associate Director.
  

• Mass spectrometry identification of proteins
  Identification of proteins will be performed by obtaining masses and fragmentation patterns of tryptic peptides and comparing these against in silico databases using MASCOT and Protein Prospector search algorithms. Protein identifications will typically begin with acquisition of peptide masses, followed by MS/MS acquisition of the ten most abundant peptides in the sample, on the Applied Biosystems 4700 Proteomics Analyzer MALDI TOF-TOF, . If necessary, or requested, parent ion fragmentation information will be obtained by initiating an acquisition on the AB QSTAR LC-ESI-QqTOF. Although the TOF-TOF produces excellent peptide fragmentation data for most peptides, some peptides ionize more efficiently, yielding better data, on the electrospray instrument.

• Intact mass analyses
  Our Voyager DE-PRO MALDI-TOF instrument is particularly useful in determining intact mass (molecular weight) of purified proteins. Intact mass data have been acquired on proteins up to 150kDa on this instrument, although resolution and mass accuracy is typically better at lower mass ranges.

• Post-translational modifications
  The Center uses fluorescent stains and 2D gel electrophoresis to allow specific imaging of phospho-proteins (ProQ-Diamond) and glyco-proteins (ProQ-Emerald). For highest probability of success, mapping of post-translational modifications by Mass Spectrometry should minimally begin with an enriched or purified preparation of the modified peptide (or protein) and the deduced amino acid sequence of the full-length polypeptide.

** Please acknowledge The Proteomics Center in any publication resulting from our services. **

For example, "The authors acknowledge The Proteomics Center at the University of Missouri-Columbia for gel electrophoresis (or mass spectrometry) services."

**While we welcome authorship on posters and manuscripts, we can only accept such authorship following detailed review of the presentation/publication by each of those members of staff included as authors. As a professional courtesy, please allow adequate time for our staff to review the material in question prior to presentation or submission.**