Welcome to the lab of Nicolas Doucet
Protein dynamics and enzyme engineering

INRS - Armand-Frappier Health & Biotechnology Center
University of Quebec
Montreal, Canada
Institut Pasteur International Network 


Media Highlights 

Structure and Vladimir Urevsky highlight our work on the conservation of protein dynamics in an enzyme superfamily.

INRS receives over $320,000 from CFI and Government of Quebec: NMR spectroscopy platform to target the development of new therapeutic agents.

Donald Gagné, a PhD student from our lab, is awarded the ADESAQ price for best Quebec thesis in health sciences: Le diplômé Donald Gagné de l’INRS reçoit un Prix d’excellence de l’ADÉSAQ.

AAAS Press Release about our work: The subtle dance of atoms influences enzyme activity.

Our research is featured on the cover of Protein Science. Click here for more details.

Protein Science Cover

Reportage télé : Le Code Chastenay

Ce site web servant principalement à faire connaître nos recherches à l'extérieur des frontières du Québec, il est rare que je prenne le temps d'écrire quelques mots en français ici. Je fais toutefois exception pour vous présenter un reportage télé à propos d'une (infime) partie de nos travaux de recherche. Ce reportage de vulgarisation scientifique, intitulé "Des arômes alimentaires écologiques fabriqués en laboratoire", a été diffusé sur les ondes de Télé-Québec le mardi 18 février 2014, dans le cadre de l'émission scientifique Le Code Chastenay. Pour ceux qui seraient intéressés à visionner le reportage, vous le retrouverez en cliquant ici.

Our main research philosophy

Can enzyme engineering benefit from the modulation of protein motions?

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

open 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.close

About our institute and facilities


What is the INRS - Armand-Frappier Health & Biotechnology Center?

Please refer to the official INRS and INRS - Armand-Frappier 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.