Speaker
Dr
Arnab Bhattacherjee
(CBBP, Lund University)
Description
Recent advances in molecular biology have revealed that many
proteins do not fold spontaneously into stable native state,
instead exist in a highly dynamic state without a specific
structure. These disordered proteins, often termed as
Intrinsically Disordered or Natively Unstructured Proteins,
play a pivot role in various cellular mechanisms by
interacting with different proteins. However, little is
known about their binding mechanism in atomistic details.
With a simple but atomistically detailed protein model, we
explore the free-energy landscape of pairs of interacting
sequences and how it is impacted by 1), variations in the
binding mechanism; and 2), the addition of disordered flanks
to the binding region. In particular, we focus on various
small helical systems and study how different modes of
associations impact kinetic and thermodynamic aspects of the
interaction.
