Perspective: Assembly and Dynamics of Integral Membrane Proteins
Membrane proteins account for 25 – 30 % of a cell’s proteome and function as fusion factors, adhesion molecules, receptors, channels etc. Their membrane-spanning helices can induce dimerization or oligomerization, specific protein/lipid interactions, drive membrane fusion, catalyze lipid flip/flop, serve as substrates for intramembrane proteases etc.
Our mission:
To understand the mechanisms by which transmembrane domains (TMDs) self-interact, their conformational dynamics, and their ability to interact with surrounding lipids.
To elucidate the functional relevance of these interconnected structural properties.
Topical questions in the lab:
Transmembrane helix-helix interactions
Transmembrane helix backbone dynamics
Transmembrane helix/lipid interactions
Functional implications of TMD-TMD interactions, TMD backbone dynamics, and TMD/lipid interactions in:
Instrumentation:
The lab hosts modern equipment to do experiments in molecular biology, biochemistry and biophysics.