Welcome to the lab of Nicolas Doucet
Protein dynamics and enzyme engineering
INRS-Institut
Armand-Frappier
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.

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.
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 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.