Calorimetric characterisation of the toxofilin–G-actin complex

Veronika Takács-Kollár, M. Nyitrai, D. Lőrinczy, G. Hild

Research output: Contribution to journalArticle

Abstract

In the present work, the thermodynamic characterisation of toxofilin–G-actin complex was completed with differential scanning calorimetry. The relative change in the under curve area of the un-complexed G-actin in the presence of varying toxofilin concentrations was used as an indirect indicator of the complex formation. The toxofilin could efficiently bind to G-actin with a KD value of 15.7 µM. Besides its binding activity, toxofilin stabilised the attached actin molecules as the Tm value of G-actin increased to 64.19 °C after the complex formation. Based on the findings, it is possible to conclude that even non-mammalian actin-binding proteins can efficiently modify the basic structural and dynamic properties of actin monomers.

Original languageEnglish
Pages (from-to)1307-1311
Number of pages5
JournalJournal of Thermal Analysis and Calorimetry
Volume131
Issue number2
DOIs
Publication statusPublished - Feb 1 2018

Fingerprint

Actins
dynamic characteristics
heat measurement
monomers
proteins
thermodynamics
scanning
curves
molecules
Microfilament Proteins
Differential scanning calorimetry
Monomers
Thermodynamics
Molecules

Keywords

  • Actin
  • Affinity
  • Cytoskeleton
  • DSC
  • Toxofilin

ASJC Scopus subject areas

  • Condensed Matter Physics
  • Physical and Theoretical Chemistry

Cite this

Calorimetric characterisation of the toxofilin–G-actin complex. / Takács-Kollár, Veronika; Nyitrai, M.; Lőrinczy, D.; Hild, G.

In: Journal of Thermal Analysis and Calorimetry, Vol. 131, No. 2, 01.02.2018, p. 1307-1311.

Research output: Contribution to journalArticle

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