Calorimetric characterization of the stable complex of myosin subfragment 1 with ADP and beryllium fluoride.
The thermal unfolding of the myosin subfragment 1 (S1) in its stable complex with ADP and beryllium fluoride (S1.ADP.BeF3-) was studied by differential scanning calorimetry. It has been shown that the structure of the S1 molecule in the S1.ADP.BeF3- complex is similar to that of S1 in its complex with ADP and orthovanadate (S1.ADP.Vi) but differs radically from that of nucleotide-free S1 and S1 in the S1.ADP complex. It is concluded that the S1.ADP.BeF3- complex can be considered, like the S1.ADP.Vi complex, a stable structural analogue of the myosin head.ADP.Pi transition state of the myosin-catalyzed ATP hydrolysis.
Bobkov
A A
AA
A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow.
Khvorov
N V
NV
Golitsina
N L
NL
Levitsky
D I
DI
D000244:Adenosine Diphosphate / Q000737:chemistry*; D000818:Animals; D001608:Beryllium / Q000737:chemistry*; D002152:Calorimetry, Differential Scanning; D005459:Fluorides / Q000737:chemistry*; D015879:Myosin Subfragments / Q000737:chemistry*; D017510:Protein Folding; D011817:Rabbits; D014638:Vanadates / Q000737:chemistry
D015879:Myosin Subfragments; D014638:Vanadates; C035982:beryllium fluoride; D000244:Adenosine Diphosphate; D001608:Beryllium; D005459:Fluorides