مرکز تحقیقات بیوشیمی و بیوفیزیک

بنـام خــدا

سخنـرانـی علمـی

Molecular Details of the Activation of Histone Deacetylase 3

Dr. Mehrnoosh Arrar, Chemistry Department, University of Buenos Aires

سه‌شنبه ۱۴/۶/۹۶ ساعت ۱۱-۱۰

آمفی تآتر مرکز تحقیقات بیوشیمی و بیوفیزیک دانشگاه تهران

Abstract:

Histones are the core proteins about which DNA is organized. The availability of specific genes is actively regulated by post-translational modifications, such as acetylation, of histone tails. Histone deacetylase 3 (HDAC3) participates in this processes by removing acetyl groups and compacting local chromatin structure. Interestingly, HDAC3 is only active in presence of a nuclear co-repressor (DAD) and, as only recently discovered, a small signaling molecule- inositol tetraphosphate. Here we use molecular dynamics simulations to shed light on the molecular details through which HDAC3 is activated and in turn modulates gene expression.

بنـام خــدا

سخنـرانـی علمـی

Molecular Basis of Thermal Stability in Truncated Hemoglobins

Dr. Leonardo Boechi, Instituto de Calculo, University of Buenos Aires

سه‌شنبه ۱۴/۶/۹۶ ساعت ۱۱-۱۰

آمفی تآتر مرکز تحقیقات بیوشیمی و بیوفیزیک دانشگاه تهران

Abstract:
Understanding the molecular mechanism through which proteins are functional at extreme high and low temperatures is one of the key issues in structural biology. To investigate this phenomenon, we have focused on two instructive truncated hemoglobins from Thermobifida fusca (Tf-trHbO) and Mycobacterium tuberculosis (Mt-trHbO); although the two proteins are structurally nearly identical, only the former is stable at high temperatures. I this talk I will describe the used of molecular dynamics simulations together with thermal melting profile measurements to establish the role of a single amino acid position in tuning the thermal stability of these proteins.