Phone: (406) 243-4408
E-mail Address: klara.briknarova@umontana.edu
Office : Cp 111
Personal Site: http://www.umontana.edu/chemistry/faculty/briknarova.htmWe use nuclear magnetic resonance (NMR) spectroscopy, biochemical and biophysical techniques to study the structure, function and dynamics of biological macromolecules. A question of particular interest is how cell identity is established and maintained at the molecular level. Brain, heart, hair or blood cells are remarkably different yet they all start with the same genes. How do different cells and tissues remember what they are, and what keeps them from going astray? Gaining insight into how cell-type specific transcription programs are determined remains a major challenge for life sciences today. Epigenetics is defined as "heritable changes in gene expression that occur without changes in DNA sequence", and it has become an area of very intensive research that has large implications for stem cell biology, development, and various human diseases including cancer. In order to understand the complex systems involved in epigenetic gene silencing, the structure, function and interactions of their components need to be elucidated.
NMR spectroscopy is well suited for these studies. It is a well established tool for structure determination of biological macromolecules and their complexes up to ~25-30 kDa. Large multidomain proteins can be conquered by division into smaller fragments. NMR methods can also be used to investigate conformational dynamics and to map ligand interaction surfaces. Recent advances in the field, including development of TROSY and applications of residual dipolar coupling to structure determination have made characterization of even larger molecules and their complexes feasible.
The NMR facility at UM contains new 500 and 600 MHz Varian NMR systems. The 600 MHz spectrometer is equipped with four channels, z-axis gradients and 13C-enhanced salt-tolerant cold probe. This spectrometer is devoted primarily to biomolecular applications. The 500 MHz spectrometer is equipped with three channels, three-axis gradients, HCN triple resonance probe, direct and indirect broadband probes, and accessories for MAS. It is available for both biomolecular studies as well as for general chemical applications.
Briknarová, K., Zhou, X., Satterthwait, A., Hoyt, D.W., Ely, K.R. and Huang, S. (2008). Structural studies of the SET domain from RIZ1 tumor suppressor. Biochem. Biophys. Res. Commun. 366, 807-813.
Briknarová, K., Nasertorabi, F., Havert, M.L., Eggleston, E., Hoyt, D.W., Li, C., Olson, A.J., Vuori, K. and Ely, K.R. (2005). The serine-rich domain from Crk-associated substrate (p130Cas) is a four-helix bundle. J. Biol. Chem. 280, 21908-21914
Derunes, C., Briknarová, K., Geng, L., Li, S., Gessner, C.R., Hewitt, K., Wu, S., Huang, S., Woods, V.I. Jr. and Ely, K.R. (2005). Characterization of the PR domain of RIZ1 histone methyltransferase. Biochem. Biophys. Res. Commun. 333, 925-934.
Briknarová, K., Åkerman, M.E., Hoyt, D.W., Ruoslahti, E. and Ely, K.R. (2003). Anastellin, an FN3 fragment with fibronectin polymerization activity, resembles amyloid fibril precursors. J. Mol. Biol. 332, 205-215.
Briknarová, K., Takayama, S., Homma, S., Baker, K., Cabezas, E., Hoyt, D.W., Li, Z., Satterthwait, A.C. and Ely, K.R. (2002). BAG4/SODD protein contains a short BAG domain. J. Biol. Chem. 277, 31172-31178.
Briknarová, K., Takayama, S., Brive, L., Havert, M.L., Knee, D.A., Velasco, J., Homma, S., Cabezas, E., Stuart, J., Hoyt, D.W., Satterthwait, A.C., Llinás, M., Reed, J.C. and Ely, K.R. (2001). Structural analysis of BAG1 co-chaperone and its interactions with Hsc70 heat shock protein. Nature Struct. Biol. 8, 349-352.
