Inter-monomer cross-linking affects the thermal transitions in F-actin

• Published in: Journal of thermal analysis and calorimetry Vol. 101; no. 2; pp. 549 - 553
• Main Authors: Könczöl, F., Lőrinczy, D., Vértes, Zs, Hegyi, G., Belagyi, J.
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Dordrecht Springer Netherlands 01.08.2010; Springer
• Subjects: Actin; Analytical Chemistry; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Chemistry; Chemistry and Materials Science; Contractile proteins; Covalence; Crosslinking; Differential scanning calorimetry; Fundamental and applied biological sciences. Psychology; Holoproteins; Inorganic Chemistry; Measurement Science and Instrumentation; Monomers; Motional; Muscle proteins; Physical Chemistry; Polymer Sciences; Proteins; Residues; Strands; Transition temperature; Actin cross-linking; DSC; Thermal stability; Differential scanning calorimetry; Thermal transition; Actin; EPR spectrometry; Contractile protein; Crosslinking; Thermal analysis; Monomer
• ISSN: 1388-6150; 1588-2926; 1572-8943
• DOI: 10.1007/s10973-010-0833-6

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.