The laboratory seeks to describe the "structure–activity–function" algorithm of proteins. Our research is located at the interface between other structure analyses methods (NMR and X-ray crystallography) and we use a combination of protein chemistry, proteomics, enzymology, and recombinant DNA techniques.
We are interested in extracellular matrix (ECM) homeostasis and the identification and characterization of post-translational modifications. Available structural and functional information concerning ECM proteins is limited due to the inherent insolubility.
Granular corneal dystrophy, Type I.
A superposition of the crystal structures of bovine TAFI (green) and porcine carboxypeptidase B (purple). Read more.
Our research is located at the interface between other structure analyses methods (NMR and X-ray crystallography) and we use a combination of protein chemistry, proteomics, enzymology, and recombinant DNA techniques.
Here you can read a popular description of the group's research results sent to the media.
