Calorimetric characterization of the stable complex of myosin subfragment 1 with ADP and beryllium fluoride.

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 Lett

journal_title

FEBS letters

authors

Bobkov AA,Khvorov NV,Golitsina NL,Levitsky DI

doi

10.1016/0014-5793(93)80485-d

subject

Has Abstract

pub_date

1993-10-11 00:00:00

pages

64-6

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(93)80485-D

journal_volume

332

pub_type

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