Vamseedhar Rayaprolu La Jolla Institute for Allergy and Immunology
2 protocols

John Peters Institute of Biological Chemistry, Washington State University, USA, USA,
1 protocol

Natasha Pence Institute of Biological Chemistry, Washington State University, USA, USA,
1 protocol

Angela Patterson Department of Chemistry and Biochemistry, Montana State University, USA, USA,
1 protocol

Brian Bothner
  • Department of Chemistry and Biochemistry, Montana State University, USA
Research focus
  • Microbiology
  • 2 Author merit


Ph.D. in Biochemistry, University of Tennessee, Memphis, USA, 2002

Current position

Director of the Proteomics, Metabolomics, and Mass Spectrometry Facility, Montana State University, Department of Chemistry and Biochemistry, Bozeman, MT (2008-present)
Professor, Montana State University, Department of Chemistry and Biochemistry, Bozeman, MT (2008-present)


Selected 9 of 63 peer-reviewed publications

  1. Hamerly, T., Heinemann, J., Tokmina-Lukaszewska, M., Lusczek, E. R., Mulier, K. E., Beilman, G. J. and Bothner, B. (2014). Bovine serum albumin as a molecular sensor for the discrimination of complex metabolite samples. Anal Chim Acta 818: 61-66.
  2. Kang, Y. S., Shi, Z., Bothner, B., Wang, G. and McDermott, T. R. (2014). Involvement of the Acr3 and DctA anti-porters in arsenite oxidation in Agrobacterium tumefaciens 5A. Environ Microbiol. (Epub ahead of print)
  3. Rayaprolu, V., Kruse, S., Kant, R., Venkatakrishnan, B., Movahed, N., Brooke, D., Lins, B., Bennett, A., Potter, T., McKenna, R., Agbandje-McKenna, M. and Bothner, B. (2013). Comparative analysis of adeno-associated virus capsid stability and dynamics. J Virol 87(24): 13150-13160.
  4. Heinemann, J., Hamerly, T., Maaty, W. S., Movahed, N., Steffens, J. D., Reeves, B. D., Hilmer, J. K., Therien, J., Grieco, P. A., Peters, J. W. and Bothner, B. (2014). Expanding the paradigm of thiol redox in the thermophilic root of life. Biochim Biophys Acta 1840(1): 80-85.
  5. Epstein, M. G., Reeves, B. D., Maaty, W. S., Fouchard, D., Dratz, E. A., Bothner, B. and Grieco, P. A. (2013). Enhanced sensitivity employing zwitterionic and pI balancing dyes (Z-CyDyes) optimized for 2D-gel electrophoresis based on side chain modifications of CyDye fluorophores. New tools for use in proteomics and diagnostics. Bioconjug Chem 24(9): 1552-1561.
  6. Maaty, W. S., Lord, C. I., Gripentrog, J. M., Riesselman, M., Keren-Aviram, G., Liu, T., Dratz, E. A., Bothner, B. and Jesaitis, A. J. (2013). Identification of C-terminal phosphorylation sites of N-formyl peptide receptor-1 (FPR1) in human blood neutrophils. J Biol Chem 288(38): 27042-27058.
  7. Kang, Y. S., Heinemann, J., Bothner, B., Rensing, C. and McDermott, T. R. (2012). Integrated co-regulation of bacterial arsenic and phosphorus metabolisms. Environ Microbiol 14(12): 3097-3109.
  8. Maaty, W. S., Selvig, K., Ryder, S., Tarlykov, P., Hilmer, J. K., Heinemann, J., Steffens, J., Snyder, J. C., Ortmann, A. C., Movahed, N., Spicka, K., Chetia, L., Grieco, P. A., Dratz, E. A., Douglas, T., Young, M. J. and Bothner, B. (2012). Proteomic analysis of Sulfolobus solfataricus during Sulfolobus Turreted Icosahedral Virus infection. J Proteome Res 11(2): 1420-1432.
  9. Furman, L. M., Maaty, W. S., Petersen, L. K., Ettayebi, K., Hardy, M. E. and Bothner, B. (2009). Cysteine protease activation and apoptosis in Murine norovirus infection. Virol J 6: 139.
2 Protocols published
Authors:  Luke Berry, Angela Patterson, Natasha Pence, John W. Peters and Brian Bothner, date: 03/20/2018, view: 6885, Q&A: 0
The protocol detailed here describes a way to perform hydrogen deuterium exchange coupled to mass spectrometry (HDX-MS) on oxygen sensitive proteins. HDX-MS is a powerful tool for studying the protein structure-function relationship. Applying this ...
Authors:  Vamseedhar Rayaprolu, Shannon Kruse, Ravi Kant, Navid Movahed, Dewey Brooke and Brian Bothner, date: 08/05/2014, view: 10500, Q&A: 1
Differential Scanning Fluorimetry (DSF) is a rapid, economical, and a straightforward technique for estimating the thermal stability of proteins. The principle involves the binding of a fluorescent dye to thermally exposed hydrophobic pockets of a ...
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