Dépôt numérique

Similarities between conformational exchange patterns in members of the ribonuclease 3 subfamily

Bernard, David N.; Gagné, Donald et Doucet, Nicolas . Similarities between conformational exchange patterns in members of the ribonuclease 3 subfamily In: 16e Symposium annuel de PROTEO, 13 Mai 2016, Université Laval, Québec, QC.

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Enzymes are increasingly being used in pharmaceutical and industrial environments, particularly as greener and more efficient alternatives to chemical catalysts. However, engineering new enzyme reactions is an arduous and inefficient process, mainly because the predictable outcome of protein engineering on 3D structure, function and dynamics remains elusive. Recent experimental evidence suggests that conformational exchange may be involved in promoting catalysis in many enzyme systems, but the mechanisms underlying this atomic flexibility remain unclear. It is still unknown whether sequence and/or structure are evolutionarily conserved to promote flexibility events linked to biological function among protein homologs. Understanding phenomena underlying protein dynamics is thus an important step in facilitating protein engineering. In order to tackle these interrogations, we have used NMR to characterize the millisecond timescale conformational exchange in various members of the ribonuclease A superfamily. While these enzymes display very similar structure, their evolutionary distance and diversified biological activities complicate flexibility-function analyses. To solve this issue, we have investigated mammalian homologs of human ribonuclease 3 (Eosinophil Cationic Protein, ECP), comparing the human enzyme with its close ECP homologs from Pongo pygmaeus and Macaca fascicularis. Our findings show that conformational exchange in the monkey enzymes strongly resembles that of their human counterpart, providing insights into the effects of sequence and phylogenetic diversity on protein dynamics. Further experiments are required to determine the exact biological roles of these enzymes and their dependence on atomic flexibility.

Type de document: Document issu d'une conférence ou d'un atelier
Informations complémentaires: Affiche scientifique
Mots-clés libres: -
Centre: Centre INRS-Institut Armand Frappier
Date de dépôt: 22 juin 2018 02:14
Dernière modification: 22 juin 2018 02:14
URI: https://espace.inrs.ca/id/eprint/5800

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