Speaker
Prof.
Ingemar André
(Center for Molecular Protein Science, Lund University)
Description
Many of the largest protein complexes in biology are
composed of a single type of subunit that is repeated a
large number of times to generate a functional assembly.
Such homomeric structures are often assembled spontaneously
from individual components through the process of
self-assembly. Research in our group is focused on the
prediction of the three-dimensional structure of homomeric
assemblies and the rational design of novel self-assembling
proteins and peptides. Over the last several years we have
developed computational methods to model the structure of
homomeric assemblies using the powerful constraint of
molecular symmetry. In this presentation I will illustrate
how these prediction methods, in conjunction with limited
experimental constraints, can be used to tackle important
problems in structural biology. The second part of the talk
will deal with the rational design of self-assembling
proteins and peptides. We combine the powerful design
template of self-assembly with structural modeling and
computational protein to design protein assemblies on an
atomic level. The final part of my talk will deal with open
questions relating to protein and peptides self-assembly
that I am interested in exploring during the workshop. In
particular, I am interested in questions relating to the
evolution of protein building blocks capable of complex
self-assembly, the assembly mechanism of multiprotein
complexes and the fine-tuning of intermolecular interactions
in protein assemblies.
