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  • 1 University of Pécs, Medical School Department of Biophysics Szigeti str. 12 Pécs 7624 Hungary
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Abstract  

The effect of phalloidin on the thermal stability of skeletal actin filaments polymerized from ADP-binding monomers was investigated with the method of differential scanning calorimetry. Phalloidin shifted the melting temperature of the ADP-F-actin from 59.1±1.0 to 80.0±1.2°C. The stabilizing effect of phalloidin propagated cooperatively along the filament. The cooperativity factor according to the applied model was 1.07±0.11. With these measurements it was possible to demonstrate that the binding of phalloidin has lower influence on the adjacent protomers in ADP- (k=1) than in ATP-actin filaments (k=3).

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  • Impact Factor (2019): 2.731
  • Scimago Journal Rank (2019): 0.415
  • SJR Hirsch-Index (2019): 87
  • SJR Quartile Score (2019): Q3 Condensed Matter Physics
  • SJR Quartile Score (2019): Q3 Physical and Theoretical Chemistry
  • Impact Factor (2018): 2.471
  • Scimago Journal Rank (2018): 0.634
  • SJR Hirsch-Index (2018): 78
  • SJR Quartile Score (2018): Q2 Condensed Matter Physics
  • SJR Quartile Score (2018): Q2 Physical and Theoretical Chemistry

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Journal of Thermal Analysis and Calorimetry
Language English
Size A4
Year of
Foundation
1969
Volumes
per Year
4
Issues
per Year
24
Founder Akadémiai Kiadó
Founder's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher
Chief Executive Officer, Akadémiai Kiadó
ISSN 1388-6150 (Print)
ISSN 1588-2926 (Online)

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