Services

Publications Online!

Please check back with us soon to view our publications as well as collaborative endeavors.

MS&P works with the OSC Bioinformatics group.

Dr. Kari Green-Church and Josh Ellis of the MS&P facility have been working with the OSC Bioinformatics group to provide cutting edge information technology advances within bioinformatics.

Third Frontier Network Representation.

Recently MS&P has attended the Ohio Third Frontier Project conference.

Please browse our services. If you are unsure about a service please contact us, and a MS&P professional will assist you.

See our services list below.

Additional information is listed, however if you require more detail please contact Dr. Kari Green-Church for more information.

	Proteomics (protein ID, sequence analysis)
	Accurate mass determination for formula conformation for organic, biological, polymer and inorganic samples.
	Mass assignment for molecular weight analysis and or conformation.
	Polymer distribution and average molecular weight analysis.
	Peptide and protein molecular weight measurement.
	Oligonucleotide molecular weight measurement and analysis.
	MS/MS for structure or sequence information
	LC-MS and capillary LC-MS
	GC-MS

		Proteomics Proteomics is a service being offered at OSU through collaboration between the CCIC-MS Facility and the Plant-Microbe Genomics Facility. The PMGF services include separation of protein mixtures on 2D gels, robotized analysis of spots and specific coring of the gels using the BioRad Proteome Works Station. Contact Kari Green-Church for more information. The Coomassie stained gel cores are sent to the CCIC Mass Spectrometry Facility for subsequent digestion, extraction and peptide fingerprint analysis using a Bruker Reflex III MALDI-TOF-MS or a Micromass Q-TOF II with capillary LC/MS/MS capabilities.
		Accurate Mass Accurate mass is used to determine the molecular weight of a sample to within 10 ppm or in other words, accurate to the third decimal point. It is used to verify a predicted molecular formula of a pure compound. The analyte is mixed with an internal standard to use as a "lock mass" or internal calibration. The Q-TOF with ESI, and LCT are available for accurate mass determination.
		MS/MS MS/MS or CID is used to determine structural or sequence information. The Esquire, and Q-TOF (ESI) can give fragment information. For ESI applications, the target molecule is isolated in the mass spectrometer and then collided with a gas to induce fragmentation. Due to the inherent nature of EI, molecules fragment as part of the ionization process. Here is an example of a tryptic peptide sequenced using the QTOF from Dr Micheal Freitas' research group.
		Polymer Distribution Polymer distribution of polar and non-polar polymers can be determined using MALDI-TOF MS. Polymers must be soluble in water or organic solvent for analysis. Our software package on the MALDI allows for calculation of Mn, Mw.
		Oligonucleotide Analysis Oligonucleotides (DNA and RNA) can be analyzed by both MALDI and ESI. As with peptides and proteins, oligos are desalted prior to analysis, all buffers and salts must be removed for mass spec analysis as it suppresses ionization and many buffers are observed as background in the mass spectrum.
		Molecular Weight Analysis A simple molecular weight analysis can determine the presence or absence of a compound, purity, relative concentration and molecular weight. We can measure molecular weights as low as 50 Da and as high as 150,000 Da (and higher, no one has submitted anything bigger). ESI, EI and MALDI can all be used for this type of sample. Polymers, peptides, proteins, oligonucleotides are typically analyzed by simple molecular weight analysis. Most of our instruments are high resolution, so you can still get isotope information with the simple molecular weight analysis.
		Protein/Peptide Analysis Protein and peptides can be analyzed by both MALDI and ESI. Peptides and proteins are desalted prior to analysis, all buffers and salts must be removed for mass spec analysis as it suppresses ionization and many buffers are observed as background in the mass spectrum. As a guideline, we would need approximately 0.5 ug of a 10 KDa protein, 2.5 ug of a 50 KDa protein and 5 - 10 ug of a 100 KDa protein for good results. Please include the sequence if known at the time of sample submission.
		GC-MS Gas chromatography (GC) and mass spectrometry (MS) make an effective combination for chemical analysis. Among its uses are drug testing and environmental contaminant identification. The sample is injected through an injection port of the GC device, the GC instrument vaporizes the sample and then separates and analyzes the various components. Each component ideally produces a specific spectral peak and the time elapsed between injection and elution is called the "retention time." The size of the peaks is proportional to the quantity of the corresponding substances in the specimen analyzed. MS identifies the separated substances by using an electron impact ionization source (EI) which breaks the molecules into charged fragments and detected by the mass analyzer. A spectral plot displays the mass of each fragment under each peak in the GC plot. The compound can be identified by the GC retention time, the parent ion and fragmentation pattern as searched by a database of known compounds. The retention time can help to differentiate between some compounds.
		LC/MS LC/MS is a very effective technique to combine peak detection with peak identification. Combining chromatography with mass spectrometry allows the chromatographer to "see inside" the chromatographic peak and to resolve co-eluting compounds of different molecular weights. Molecular weight information can identify predicted unknowns with better certainty and identify true unknowns by obtaining a "fingerprint' mass spectrum or fragmentation from CID and searching against commercial databases of spectra.

Mass Spectrometry & Proteomics The Ohio State University