Latest News

March 2012

We characterized a new enzyme from the soil-dwelling bacterium S. coelicolor, which we are now currently trying to use as an industrial catalyst for the production of chemical flavours. Our initial report is now published in PLoS ONE.

January 2012

Our newest investigation of artificial metalloenzyme complexes for enantioselective epoxidation is now published in Chembiochem. This work was performed in collaboration with our French colleagues Jean-Pierre Mahy and Rémy Ricoux (Université Paris-Sud 11).

October 2011

Nick is a new member of the FRQS-sponsored Groupe de Recherche Axé sur la Structure des Protéines (GRASP). More info here.

 

Can enzyme engineering benefit from the modulation of protein motions?

Doucet, N. (2011) Protein & Peptide Letters, 18(4), 336-343.

Despite impressive progress in protein engineering and design, our ability to create new and efficient enzyme activities remains a laborious and time-consuming endeavor. In the past few years, intricate combinations of rational mutagenesis, directed evolution and computational methods have paved the way to exciting engineering examples and are now offering a new perspective on the structural requirements of enzyme activity.

However, these structure-function analyses are usually guided by the time-averaged static models offered by enzyme crystals and NMR structures, which often fail to describe the functionally relevant 'invisible states' adopted by proteins in space and time. To alleviate such limitations, NMR relaxation dispersion experiments coupled to mutagenesis studies have recently been applied to the study of enzyme catalysis, effectively complementing 'structure-function' analyses with 'flexibility-function' investigations.

In addition to offering quantitative, site-specific information to help characterize residue motion, these NMR methods are now being applied to enzyme engineering purposes, providing a powerful tool to help characterize the effects of controlling long-range networks of flexible residues affecting enzyme function.

About our Institute, Lab and Facilities

What is INRS and INRS-Institut Armand-Frappier?

Please refer to the official INRS and INRS-IAF websites for more information on our institute and research facilities.

Who was Armand Frappier?

To learn more about the man who founded the institute (Armand Frappier, 1904-1991), read this short profile, watch this NFB documentary (in French) and/or visit the Armand-Frappier Museum.

Principal Investigator

Nicolas Doucet obtained his B.S. in biochemistry from Laval University (B.S. Biochemistry, 2000) and successively completed a master's degree (M.S. Biochemistry, 2004) and a doctoral thesis in enzyme engineering with Joelle N. Pelletier at the University of Montreal (Ph.D. Biochemistry, 2007).

After completing a protein NMR postdoctoral fellowship in the Department of Chemistry at Yale University (with J. Patrick Loria, 2007-2010), he joined the faculty at INRS Institut Armand-Frappier in 2010.