Department of Chemistry

CMS Services

Faculty seeking access to mass spectrometry analysis are often confused by the fact that there are other MS laboratories and instruments located in the ILSB, specifically the Laganowsky and Russell research groups; however, these units are not formally part of the CBMSC. In addition, the TAMU NIH P41 (funded July 1, 2018) "Resource in Native Mass Spectrometry-Guided Structural Biology", which includes laboratories at Ohio State University (lead unit) and West Virginia University, provide unique, cutting-edge mass spectrometry capabilities. The Laganowsky and Russell research programs serve as "Driving Biological Projects" (Laganowsky) and "Technology Research and Development Programs" (Russell) as components of the P41 grant. The NIH P41 "Resource" has received partial funding from the Department of Chemistry, College of Science and OVPR; consequently, these research capabilities are made available on a collaborative basis to TAMU researchers. Because these instruments are not formally part of the CBMSL, we have no mechanism to recover operational, maintenance and analysis costs. We currently have a number of collaborations that have produced publications in high-impact journals, and these are the kinds of products that serve as the basis for competitive federal grants that enhance TAMU's stature and interdisciplinary training/education of students.

Protein Identification

Protein identification is most commonly accomplished by proteolytic digestion followed by MS analysis. Sample are typically submitted as gel bands, pelleted pure proteins, or proteins in solution without detergents or glycerol (preferably in 25mM Ammonium Bicarbonate buffer, pH=7-8). Samples are enzymatically digested, typically with mass spec grade trypsin, and analyzed by either MALDI-TOF-MS/MS or nano-capillary HPLC/MSMS. The resulting MS and MS/MS data can then be queried against a specific database for peptide and protein identification.

Exact Mass Analysis for Proteins

Clients often need to know the exact mass of a purified protein. Samples need to be in Na and K free buffers, in the absence of detergents, chaotrophic agents, and glycerol. We recommend ammonium acetate or ammonium bicarbonate buffers if they are required.

Intact Protein Complex Mass Determination

Masses of purified protein complexes and subunit composition can also be determined in our facility. This is non-routine work and we highly recommend a consultation before submitting your samples.

Proteomic Analysis

Complex mixtures of proteins can also be identified by MS. However, protein ID requires LCMS for analysis. Prefractionation of the proteins, such as 1D SDS-PAGE can be used to increase the numbers of proteins identified by the experiment. Other approaches include separation of digest proteins peptides using high pH LC, collecting fractions and running those fractions by low pH LCMS. Yet another approach is to run long gradients using normal reverse phase chromatography-MS. Set up a consultation and we can decide which is best for you. We also offer semi-quantitative techniques, either label-free or labeling for your proteomic analysis.

Posttranslational Modification Site Determination

Starting with a single highly purified protein, either as a gel band or purified protein, multiple sites of modification, eg. Glycosylation, phosphorylation, acetylation and others, can be determined. This process is non-routine and typically requires multiple digestion enzymes. We recommend you set up a consultation before beginning this work.

CMS Rates


Standard analysis by Electron Ionization (EI), Chemical Ionization (CI), Atmospheric Pressure Chemical Ionization (APCI), Electrospray Ionization (ESI), and Matrix Assisted Laser Desorption Ionization (MALDI).

Customer Type Hourley Rate*
Texas A&M University (all departments and campuses) $85
Other Universities $85
Industry $200/negotiable

*2 samples/hr is ideal


MS/MS analysis of peaks in ESI, APCI, and MALDI spectra.

Customer Type Hourley Rate*
Texas A&M University (all departments and campuses) $85
Other Universities $85
Industry $200

CMS Submissions


To submit a sample to the CMS, fill out one of the following submission forms:

Fill out the form by providing as much information as you can. Attach your sample to the submission form. If you are on campus, samples can be dropped off in room 1195 or 1145 of the ILSB.

If your sample requires special storage, please see the Sample Submission Guidelines.

If you are submitting a sample from outside Texas A&M University, please contact us before you submit your sample. Use the express shipping address provided to send your samples.

New Customers

If you are submitting samples for the first time and you are located outside the Texas A&M University, please fill out Customer Information Sheet and send it to us. Once the form is received and approved, you can start using the facility.

CMS Forms