Conclusion

The DSC approach offers new unique opportunities for structural and functional studies on muscle proteins. It allows very clear revealing and following detailed investigation of global structural changes that occur in the myosin head during ATPase reaction and due to interaction with actin. This approach, in combination with other methods, allows to investigate long-distance communication pathways between functionally important but spatially far regions in the myosin head. DSC also provides a new and promising approach for studying of highly cooperative conformational changes in actin filaments induced by actin-binding proteins. Moreover, DSC in combination with other methods is very useful for structural characterization of tropomyosin on the surface of actin filaments. Thus, DSC studies on muscle proteins offer a promising approach to probe and investigate structural changes which play an important role in functioning of these proteins.

Acknowledgements

I thank my colleagues and friends participated in DSC experiments on muscle proteins from 1989 up to now: Valery Shnyrov, Nina Golitsina, Olga Nikolaeva, Nikolai Khvorov, Andrey Bobkov, Irina Dedova, Elena Rostkova, Dmitrii Pavlov, Victor Orlov, Mikhael Ponomarev, Olga Kaspieva, Elena Kremneva, Valeriya Mikhailova, Lubov' Shakirova, Elena Siletskaya, and Eugene Zubov.

This work was supported in part by the Russian Foundation for Basic Research (Grant 03-04-48237), by the Program for the Support of the Leading Scientific Schools in Russia (Grant NSH-813.2003.04), by the Program on Physico-Chemical Biology of Russian Academy of Sciences, and by the Welcome Trust (Grant 066115/Z/01/Z).

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