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Calorimetric characterization of the stable complex of myosin subfragment 1 with ADP and beryllium fluoride
Author(s) -
Bobkov Andrey A.,
Khvorov Nikolai V.,
Golitsiina L.,
Levitsky Dmitrii I.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80485-d
Subject(s) - myosin , chemistry , characterization (materials science) , fluoride , beryllium , biophysics , biochemistry , inorganic chemistry , materials science , biology , nanotechnology , organic chemistry
The thermal unfolding of the myosin subfragment 1 (S1) in its stable complex with ADP and beryllium fluoride (S1 · ADP · BeF 3 − ) was studied by differential scanning calorimetry. It has been shown that the structure of the S1 molecule in the S1 · ADP · BeF 3 − complex is similar to that of S1 in its complex with ADP and orthovanadate (S1 · ADP · V i but differs radically from that of nucleotide‐free S1 and S1 in the S1 · ADP complex. It is concluded that the S1 · ADP · BeF 3 − complex can be considered, like the S1 · ADP · V i complex, a stable structural analogue of the myosin head · ADP · P i transition state of the myosin‐catalyzed ATP hydrolysis.