| Autor: |
Bobkov, Andrey A., Khvorov, Nikolai V., Golitsina, Nina L., Levitsky, Dmitrii I. |
| Zdroj: |
FEBS Letters; October 1993, Vol. 332 Issue: 1-2 p64-66, 3p |
| Abstrakt: |
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 · Vibut 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 · Vicomplex, a stable structural analogue of the myosin head · ADP · Pitransition state of the myosin‐catalyzed ATP hydrolysis. |
| Databáze: |
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