SEMINAR
OF PHYSICS OF THE LIVING STATE
(Applied Physics Scientific Section)
2010 Academic Year
Thursday, 2 September 2010
Oppenheimer Meeting
Room, Second Floor, Leonardo Building
Time: 15.30
A novel method for analyzing differential scanning calorimetry data of multi-domain proteins (*)
Abdolkhalegh Bordbar (**)
Laboratory of Biophysical Chemistry, Department of Chemistry,
University of Isfahan, Isfahan, Islamic Republic of Iran.
Summary: Protein thermal
stability is important for therapeutic proteins, both influencing the
pharmacokinetic and pharmacodynamic properties and for stability during
production and shelf life of the final product. Differential Scanning
Calorimetry (DSC) is one of the best techniques for investigation of
thermal stability of proteins. However, the analysis of thermal
profiles of multi-domain proteins is one of the challenges we still
have to face. For overcoming these difficulties, in the seminar a novel
method will be discussed by using the effective ΔG concept. The
method has been developed for the analysis of DSC profiles of
multi-domain proteins. This procedure has been successfully applied for
the analysis of DSC thermograms of pepsin. The results we have
obtained have been confirmed by several other valuable techniques.
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(**) Biodata: Professor Abdol-khalegh Bordbar
graduated in Biophysical Chemistry at the University of
Tarbiat-Modarres with a distinguished degree in 1997. After graduating,
he has worked as an Assistant Professor at the Department of Chemistry,
University of Isfahan, Isfahan, Iran.
Since 2007 he is Professor at
this university. He was distinguished researcher in Isfahan university
in 2007. He has published more than 60 international papers in the area
of Biophysical Chemistry and supervised many MSc and PhD students. His
main interests are related to interaction of ligands to
biomacromolecules, structure-function relationship in biological
systems, protein stability and interaction of anticancer drugs with
transport proteins and DNA.
