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Structural and functional studies of muscle proteins by using differential scanning calorimetry

  • Chapter
The Nature of Biological Systems as Revealed by Thermal Methods

Part of the book series: Hot Topics in Thermal Analysis and Calorimetry ((HTTC,volume 5))

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.

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  1. A. N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky prosp. 33, Moscow, 119071

    D. I. Levitsky

  2. A. N. Belozersky Institute of Physico-Chemical Biology, M. V. Lomonosov Moscow State University, Moscow, 119992, Russia

    D. I. Levitsky

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  1. Biophysical Department, Faculty of Medicine, University of Pécs, Hungary

    Dénes Lörinczy

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Levitsky, D.I. (2004). Structural and functional studies of muscle proteins by using differential scanning calorimetry. In: Lörinczy, D. (eds) The Nature of Biological Systems as Revealed by Thermal Methods. Hot Topics in Thermal Analysis and Calorimetry, vol 5. Springer, Dordrecht. https://doi.org/10.1007/1-4020-2219-0_6

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