Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Bobkov AA,Khvorov NV,Golitsina NL,Levitsky DIdoi
10.1016/0014-5793(93)80485-dsubject
Has Abstractpub_date
1993-10-11 00:00:00pages
64-6issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(93)80485-Djournal_volume
332pub_type
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