Authors:
F. Könczöl Institute of Forensic Medicine, Faculty of Medicine, University of Pecs, Szigeti u. 12, Pecs, 7633 Hungary

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D. Lőrinczy Biophysical Department, Faculty of Medicine, Institute of Biophysics, University of Pecs, Szigeti u. 12, Pecs, 7633 Hungary

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Zs. Vértes Institute of Physiology, Faculty of Medicine, University of Pecs, Szigeti u. 12, Pecs, 7633 Hungary

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G. Hegyi Department of Biochemistry, Eötvös University, Pázmány Péter sétány 1, Budapest, 1117 Hungary

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J. Belagyi Biophysical Department, Faculty of Medicine, Institute of Biophysics, University of Pecs, Szigeti u. 12, Pecs, 7633 Hungary

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Abstract  

Chemical cross-links which covalently connected the Cys-374 and Glu-41 residues of adjacent monomers in the same strand of F-actin were used to follow the consequences of the modification for the motional and structural properties of the actin filaments. DSC measurements reported that the inter-monomer cross-links shifted the thermal transition temperature and affected strongly the cooperativity of the transition in comparison with uncross-linked F-actin. Addition of HMM to F-actin induced significant decrease of the transition temperature to lower value from 69.4 to 67. 5 °C.

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Journal of Thermal Analysis and Calorimetry
Language English
Size A4
Year of
Foundation
1969
Volumes
per Year
1
Issues
per Year
24
Founder Akadémiai Kiadó
Founder's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher
Chief Executive Officer, Akadémiai Kiadó
ISSN 1388-6150 (Print)
ISSN 1588-2926 (Online)

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