Welcome to the Martin Willemoës website

In the Martin Willemoës group we are interested in enzymes from both a structure-function perspective and from an evolutionary perspective. We engineer enzymes to have new substrate specificities either by rational sidechain substitutions or by the use of genetic selection systems based on synthetic biology that allows us to search for new enzyme properties in random mutation libraries.

We also host a microcalorimetry facility allowing for thermodynamic analysis in small volume samples. We are using it to study the kinetics of enzyme catalyzed reactions, protein-protein interactions and protein-ligand interactions and wellcome proposals for collaboration in this field.

As a student you are also very welcome to stop by my office to discuss project proposals with me. Read more about how to join the group on the Section for Biomolecular Sciences homepage on joining the labs.

Research interests

We combine enzymology and enzyme engineering with the development of genetic selection systems based on the growth of Escherichia coli to evolve new enzyme activities directed towards e.g. new peptide recognition sequences (HIV protease), deglycosylation of glyco-proteins and the mechanisms that guide the specificity excerted by binding modules and -sites in reactions catalysed by maybe otherwise promiscuous endo- or exoglycosidases. These projects in part serve to make us wiser with respect to understanding how the modification of enzymes can lead to a whole new tool-box addressing the problems faced with green chemistry, industrial waste etc.

Research projects

We are working on the following projects:

Specificity and drug resistance of virus proteases
Glycosidase engineering

Specificity and drug resistance of virus proteases

We also try to gain insight into e.g. the complex rules that govern substrate specificity or development of resistance to anti-HIV drugs in HIV protease. Likewise, we also work on the M2 proton transport channel of the influenza virus to elucidate the mechanisms by which resistance to drugs by mutation also takes place for this channel. Hopefully, we may be able to predict the efficiency of drugs from the combination of data and computational chemistry. These projects take place in a close collaboration with Assoc. Prof. Kresten Lindorff-Larsen and Prof. Jakob R. Winther.

Glycosidase engineering

We engineer glycosidases to catalyse reactions on new substrates or act as glycan transferases to glycosylate medically important peptides etc.

Location

Our lab is located on the 2nd floor, building 3 of the Copenhagen Biocenter (map), close to the centre of Copenhagen. It takes less than 1 hour to travel from Copenhagen's airport to our lab, by train or subway (from the airport to Nørreport station, a 20 minute journey, with trains every 10 minutes) and bus (bus 150S from Nørreport to the stop called "Fredrik Bajers Plads" in the intersection of Tagensvej and Nørre Allé, a 10 minute journey, with buses every 6-8 minutes). From there it is a few minutes walk.