Eur Biophys J
October 2013
Formins are highly conserved proteins that are essential in the formation and regulation of the actin cytoskeleton. The formin homology 2 (FH2) domain is responsible for actin binding and acts as an important nucleating factor in eukaryotic cells. In this work EPR and DSC were used to investigate the properties of the mDia1-FH2 formin fragment and its interaction with actin.
View Article and Find Full Text PDFIn this study, experiments were carried out in the conventional and saturation-transfer electron paramagnetic resonance (EPR) time domains to explore the effect of mDia1-FH2 formin fragments on the dynamic and conformational properties of actin filaments. Conventional EPR measurements showed that addition of formin to actin filaments produced local conformational changes in the vicinity of Cys-374 by increasing the flexibility of the protein matrix in the environment of the label. The results indicated that it was the binding of formin to the barbed end that resulted in these conformational changes.
View Article and Find Full Text PDFJ Therm Anal Calorim
March 2009
The effect of phalloidin on filaments polymerized from ADP-actin monomers of the heart muscle was investigated with differential scanning calorimetry. Heart muscle contains alpha-skeletal and alpha-cardiac actin isoforms. In the absence of phalloidin the melting temperature was 55 degrees C for the alpha-cardiac actin isoform and 58 degrees C for the alpha-skeletal one when the filaments were generated from ADP-actin monomers.
View Article and Find Full Text PDFPatients' response to the relocation of an established practice from the community to a hospital-based teaching unit was measured at the end of one year. Questionnaires were sent to a randomly selected group of adult patients, asking about their impressions of the new clinic or their reasons for switching practices. The major reason cited for changing practices was the change of geographic location, rather than the change from community to teaching practice.
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