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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Purdue Univ, Sch Mech Engn, 585 Purdue Mall, W Lafayette, IN 47907 USAPurdue Univ, Sch Mech Engn, 585 Purdue Mall, W Lafayette, IN 47907 USA
Jung, Wonyeong
Murrell, Michael P.
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Yale Univ, Dept Biomed Engn, 55 Prospect St, New Haven, CT 06520 USA
Yale Univ, Syst Biol Inst, 840 West Campus Dr, West Haven, CT 06516 USAPurdue Univ, Sch Mech Engn, 585 Purdue Mall, W Lafayette, IN 47907 USA
Murrell, Michael P.
Kim, Taeyoon
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Purdue Univ, Weldon Sch Biomed Engn, 206 S Martin Jischke Dr, W Lafayette, IN 47907 USAPurdue Univ, Sch Mech Engn, 585 Purdue Mall, W Lafayette, IN 47907 USA