caa a22 4500 463190351 CHVBK 20180406164907.0 cr unu---uuuuu 170326e20071101xx s 000 0 eng 10.1007/s10973-006-7728-6 doi (NATIONALLICENCE)springer-10.1007/s10973-006-7728-6 Intermediate states of myosin head during atp hydrolysis cycle in psoas muscle fibres by EPR and DSC [Elektronische Daten] A review [D. Lőrinczy, J. Belágyi] Force generation in muscle during contraction arises from direct interaction of the two main protein components of the muscle, myosin and actin. The process is driven by the energy liberated from the hydrolysis of ATP. In the presence of CaATP the energy released from hydrolysis produces conformational changes in myosin and actin, which can be manifested as an internal motion of myosin head while bound to actin. It is suggested that myosin heads attached to actin produce conformational changes during the hydrolysis process of ATP, which results in a strain in the head portion of myosin in an ATP-dependent manner. These structural changes lead to a large rotation of myosin neck region relieving the strain. Paramagnetic probes and EPR spectroscopy provide direct method in which the rotation and orientation of specifically labelled proteins can be followed during muscle activity. In order to find correlation between local and global structural changes in the intermediate states of the ATPase cycle, the spectroscopic measurements were combined with DSC measurements that report domain stability and interactions. In the review a detailed description of the application of EPR and DSC techniques in muscle protein research will be given. The measurements show that the small local structural changes detected by EPR after nucleotide binding influence the global structure of protein system responsible for muscle contraction. Springer Science+Business Media, LLC., 2007 DSC nationallicence EPR nationallicence intermediate states of ATP hydrolysis nationallicence muscle fibre nationallicence Lőrinczy D. Institute of Biophysics, Faculty of Medicine, University of Pécs, Szigeti str. 12, H-7624, Pécs, Hungary aut Belágyi J. Institute of Biophysics, Faculty of Medicine, University of Pécs, Szigeti str. 12, H-7624, Pécs, Hungary aut Journal of Thermal Analysis and Calorimetry Springer US; http://www.springer-ny.com 90/2(2007-11-01), 611-621 1388-6150 90:2<611 2007 90 10973 https://doi.org/10.1007/s10973-006-7728-6 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10973-006-7728-6 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Lőrinczy D. Institute of Biophysics, Faculty of Medicine, University of Pécs, Szigeti str. 12, H-7624, Pécs, Hungary aut NATIONALLICENCE 700 1- Belágyi J. Institute of Biophysics, Faculty of Medicine, University of Pécs, Szigeti str. 12, H-7624, Pécs, Hungary aut NATIONALLICENCE 773 0- Journal of Thermal Analysis and Calorimetry Springer US; http://www.springer-ny.com 90/2(2007-11-01), 611-621 1388-6150 90:2<611 2007 90 10973 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer