Molecular mechanisms of function and dysfunction of skeletal muscle. I am interested in the molecular mechanism of muscle contraction, particularly in the mechanism of interactions between actin and myosin. My working hypothesis is that muscle contractility results from structural transitions in actin and myosin. I am using optical spectroscopy to detect functionally relevant structural transitions in actin. I apply my basic research approaches to investigate molecular mechanisms of muscle dysfunction, with focus on the age-related weakening of muscle. I am pursuing the hypothesis that aging of muscle is associated with the oxidative modification of actin and myosin by reactive oxygen species and subsequent inhibition of biological functions.

Prochniewicz E, Lowe DA, Spakowicz D, Higgins L, Oconor K, Thompson LV, Ferrington DA, Thomas DD.  2007. Functional, structural and chemical changes in myosin associated with hydrogen peroxide treatment of skeletal muscle fibers. Am J Physiol Cell Physiol. In press.

Prochniewicz E, Thompson LV, Thomas DD.  2007. Age-related decline in actomyosin structure and function. Exp Gerontol. 42: 931-8.

Korman VL, Anderson SE, Prochniewicz E, Titus MA, Thomas DD.  2006. Structural dynamics of the actin-myosin interface by site-directed spectroscopy. J Mol Biol. 356: 1107-17.

Prochniewicz E, Janson N, Thomas DD, De la Cruz EM. 2005.  Cofilin increases the torsional flexibility and dynamics of actin filaments. J Mol Biol. 353: 990-1000.

Prochniewicz E, Thomas DD, Thompson LV. Age-related decline in actomyosin function. 2005. J Gerontol A Biol Sci Med Sci. 60: 425-31.

Prochniewicz, E., Thomas, D.D. and Thompson, LV. 2004. Age-related decline in actomyosin function. Submitted to J. Biol. Chem.