Low complexity regions within intrinsically disordered regions in protein sequences: function, structure and evolution.
Abstract:
Non-globular regions in proteins are mostly intrinsically disordered regions (IDRs). While globular domains are structurally stable and can be found as evolutionarily conserved units with
associated functions, disordered regions represent a challenge for computational methods that attempt to classify them and predict their structural properties and functions. To address
this issue, we have been focusing on regions with low complexity often found within IDRs, that is, composed of only a few types of amino acids. Some of these are homorepeats, short
tandem repeats and compositionally biased regions. We are trying to characterize their properties and evolutionary features to find in what contexts the might gain structure and/or function,
and how they came to be.
Talk:
Low complexity regions within intrinsically disordered regions in protein sequences: function, structure and evolution.
Speaker:
Prof. Dr. Miguel Andrade, Faculty of Biology of the Johannes Gutenberg University Mainz
When:
Thursday, October 8, 2026, 3:00 pm
Where:
Seminar Room „Nucleus“, FLI 1, Beutenbergstraße 11, Jena
Host:
Mark Olenik
This seminar will be held as an in-person event.