The effect of mouse twinfilin-1 on the structure and dynamics of monomeric actin

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

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5 Citations (Scopus)


The effect of twinfilin-1 on the structure and dynamics of monomeric actin was investigated with fluorescence spectroscopy and differential scanning calorimetry experiments. Fluorescence anisotropy measurements proved that G-actin and twinfilin-1 could form a complex. Due to the formation of the complexes the dissociation of the nucleotide slowed down from the nucleotide-binding pocket of actin. Fluorescence quenching experiments showed that the accessibility of the actin bound ϵ-ATP decreased in the presence of twinfilin-1. Temperature dependent fluorescence resonance energy transfer and differential scanning calorimetry experiments revealed that the protein matrix of actin becomes more rigid and more heat resistant in the presence of twinfilin-1. The results suggest that the nucleotide binding cleft shifted into a more closed and stable conformational state of actin in the presence of twinfilin-1.

Original languageEnglish
Pages (from-to)840-846
Number of pages7
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Issue number7
Publication statusPublished - Jul 1 2016



  • Actin
  • Differential scanning calorimetry
  • Fluorescence spectroscopy
  • Mouse twinfilin-1

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Analytical Chemistry
  • Molecular Biology

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