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Workshop / Seminar

CHE 598 Seminar

Spark 335 and Floyd 224 on the Tri-Cities campus
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Dr. Vitold E. Galkin professional headshot

About the event

Dr. Vitold E. Galkin, received his BS in Chemistry and his MS in Biology from Saint-Petersburg State Technological Institute in Russia. He then went on to receive his Ph.D. in Biochemistry and Cell Biology from the Institute of Cytology, Russian Academy of Sciences in Saint-Petersburg Russia.  Over the last 15 years Dr. Galkin has been working on the structure of F-actin and its complexes with actin binding proteins (ABPs). During his post-doctoral training in the Department of Biochemistry and Molecular Genetics at the University of Virginia, Dr. Galkin contributed to the development of the single particle approach to the 3D reconstruction of the helical assembles pioneered by Dr. Egelman. This method allows one to deal with intrinsically heterogeneous filamentous complexes without averaging over different structural modes and thus avoiding artefactual results. Dr. Galkin’s success in the application of this method to solving structures of helical polymers has reflected in 47 scientific papers published over the last decade in peer reviewed journals including Science and Nature Structural and Molecular Biology. Currently, Dr. Galkin is serving as an Associate Professor at Eastern Virginia Medical School. Dr. Galkin’s lab focuses on the understanding of fundamental aspects of cardiac muscle regulation, in particular, how Ca2+-induced translocation of tropomyosin on the surface of cardiac thin filament regulates heart contraction.

Cryo Electron Microscopy – A Promising Tool in Curing Cardiovascular Diseases.

Muscle contraction is required for critical physiological functions. It relies on sliding of myosin-based thick filaments and thin filaments comprised of actin, tropomyosin and troponin. The interaction between the thick and thin filaments (actomyosin interaction) is regulated through a translocation of tropomyosin cable on the surface of the thin filament by the troponin complex in response to Ca2+. Cardiac myosin binding protein-C (cMyBP-C), an intrinsic protein of the thick filament, is a key regulator of actomyosin interactions, essential for both normal cardiac contraction and for increased cardiac contractility in response to inotropic stimuli. Mutations in MYBPC3, the gene encoding cMyBP-C, are the single most common genetic cause of hypertrophic cardiomyopathy (HCM). For a long time the mechanism of Ca2+-dependent activation of the thin filament remained poorly understood, while the molecular details of cMyBP-C interaction with the thin filament were unknown. The development of cryo electron microscopy (cryo-EM) tools allows for the first time to visualize the movement of the tropomyosin cable on the surface of the thin filament to better understand cardiac muscle regulation and to reveal the mechanism of activation of the thin filament by cMyBP-C.