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Thermal denaturation of myosin subfragment 1 modified at residue Lys-83 and its changes induced by nucleotide binding


, : Thermal denaturation of myosin subfragment 1 modified at residue Lys-83 and its changes induced by nucleotide binding. Biochemistry (Moscow) 60(7): 835-842

The effects of trinitrophenylation of lysyl residues of rabbit skeletal myosin subfragment 1 (S1) on thermal denaturation of S1 in the absence of nucleotides, in the presence of ADP, and in complexes of S1 with ADP and P-i analogs - orthovanadate (V-i) or beryllium fluoride (BeF-x) - have been studied by differential scanning calorimetry. It has been shown that lysyl trinitrophenylation significantly affects the thermal stability of S1, changes the S1 domain structure, promotes the decomposition of the S1 cntdot ADP cntdot V-i and S1 cntdot ADP cntdot BeF-x complexes, and prevents to a great extent the structural changes of the S1 molecule induced by the formation of the S1 cntdot ADP cntdot V-i complex, but has practically no influence on S1 thermal stability in the S1 cntdot ADP and S1 cntdot ADP cntdot BeF-x complexes. We demonstrate that the effects of trinitrophenylation on the S1 structure are mainly caused by specific modification of the epsilon-amino group of the Lys-83 residue.

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