A link between viscoelastic mechanics and biochemical function of proteins
Date:
Colloquia
Time: 11:00-12:15
Location: Gerhard M.J. Schmidt Lecture Hall
Lecturer: Prof. Tsvi Tlusty
Organizer: Faculty of Chemistry
Details: Department of Physics,
National University in Ulsan, South Korea
Abstract: Our starting point is the idea that specific regions in the protein evolve to
b ... Read more Our starting point is the idea that specific regions in the protein evolve to
become flexible viscoelastic elements facilitating conformational changes
associated with function, especially allostery. Simple theories show how
these regions can emerge through evolution and indicate that they are
easily identified by amino acid rearrangement upon binding (i.e., shear
motion). Surprisingly, AlphaFold can also identify such regions by
computing the shear induced by a single or a few mutations. With these
methods, we have tested the concept of shear and its functional relevance
in a variety of proteins. I will present recent results from an experimental
study of the enzyme guanylate kinase linking shear, large scale motions,
and catalytic function. Altogether, the present findings paint a physical
picture of proteins as viscoelastic machines with sequence encoded
specifications, and we will discuss its general implications for
understanding proteins and designing new ones.Close abstract
