High Resolution Protein Mass Measurement

Precise mass measurement

Precise molecular weights can be determined for proteins (including glycoproteins) by mass spectrometry. Mass spectrometry is particularly powerful for the identification of post-translational modifications. In this particular case, the location of the post-translational modification will not be known but the number of disulfide bonds on a protein without any other PTMs can be identified. The sequence of a protein produced in bacteria can also be validated this way.

In order to measure the molecular weight of the protein, the protein needs to be devoid of any detergents and is usually exchanged in a denaturing solution consisting of water/ methanol/ acetic acid (48/50/2 in percentage)



Charge state distribution

Another application of intact protein mass measurement is looking at the charge state distribution of a protein after acid or heat denaturation. The charge state distribution correlates with the unfolding of the protein.


Please contact the facility at lmbcr_help@ouhsc.edu or Dr. Virginie Sjoelund if you have any questions or need help choosing a service to fit your experiment.

For online submission navigate to iLabs for the core login page: https://ouhsc.corefacilities.org/

Any problems with iLab read the help manuals below: