John Stamm
| Office: |
BSBE 1-138 |
| Phone: |
(612) 626-0113 |
| Fax: |
(612) 624-0632 |
| Mail: |
312 Church St.
Minneapolis, MN 55455
|
| Email: |
js@ddt.biochem.umn.edu |
Research Interests:
My research focuses on the protein-protein interactions involved in phospholamban's
(PLB) regulation of the cardiac sarcoplasmic reticulum Ca-ATPase. Specifically,
I employ EPR spectroscopy to probe the protein-protein interactions involved
in phospholamban's oligomeric structure in the membrane as well as interactions
between PLB and the Ca-ATPase. Through site-directed mutagenesis I introduce
spin-labeling sites in PLB enabling the study of different specific sites by EPR. I
visualize and interpret the information gained through EPR using computational
modeling techniques. Techniques: electron paramagnetic resonance spectroscopy,
computational molecular modeling, molecular biology.
Publications:
Thomas, D.D., L.G. Reddy, C. B. Karim, M. Li, R. Cornea, J.M. Autry, L.R. Jones,
and J.D. Stamm. 1998. Direct spectroscopic detection of molecular dynamics and
interactions of the calcium pump and phospholamban. Ann. New York Acad. Sci.,
853:186-195.
Karim, C.B., J.D. Stamm, J. Karim,L.R. Jones, and D.D. Thomas. 1998. Cysteine
reactivity and oligomeric structures of phospholamban and its mutants. Biochemistry,
37:12074-12081.
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