Interaction of F‐actin with phosphate analogues studied by differential scanning calorimetry
- 29 August 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 351 (1) , 15-18
- https://doi.org/10.1016/0014-5793(94)00801-9
Abstract
The thermal unfolding of F‐actin and the changes induced in it by the binding of phosphate analogues were studied by differential scanning calorimetry. It is shown that the conformation of actin is drastically altered by interaction with beryllium fluoride or aluminium fluoride, while the effects of vanadate and phosphate are negligible. The effect of beryllium fluoride on the F‐actin structure, as reflected in a significant increase of the actin thermal stability, is much more pronounced in the presence of Mg2+ than in the case of F‐actin polymerized by KCl or LiCl in the absence of Mg2+. It is concluded that differential scanning calorimetry is a very convenient method for probing the conformational changes in F‐actin caused by the interaction with phosphate analogues.Keywords
This publication has 14 references indexed in Scilit:
- Actin conformation is drastically altered by direct interaction with membrane lipids: A differential scanning calorimetry studyBiochemistry, 1993
- Calorimetric characterization of the stable complex of myosin subfragment 1 with ADP and beryllium fluorideFEBS Letters, 1993
- Observation of multiple myosin subfragment 1-ADP-fluoroberyllate complexes by fluorine-19 NMR spectroscopyBiochemistry, 1993
- A Conformational Change in the Actin Subunit Can Change the Flexibility of the Actin FilamentJournal of Molecular Biology, 1993
- Effects of nucleotide binding on thermal transitions and domain structure of myosin subfragment 1European Journal of Biochemistry, 1992
- Structural basis for the destabilization of F-actin by phosphate release following ATP hydrolysisJournal of Molecular Biology, 1992
- Lithium increases actin polymerization rates by enhancing the nucleation stepJournal of Molecular Biology, 1991
- Atomic structure of the actin: DNase I complexNature, 1990
- Effects of ions and pH on the thermal stability of thin and thick filaments of skeletal muscle: high-sensitivity differential scanning calorimetric studyBiochemistry, 1990