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UID:69dad5bcce234
DTSTAMP:20260411T191404
DTSTART:20180201T113000
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TRANSP:OPAQUE
DTEND:20180201T113000
URL:https://murmitoyen.com/events/vanille/udem/detail/804021-seminaire-char
 lie-fehl-university-of-oxford
LOCATION:Pavillon Roger-Gaudry \, 2900\, boul. Édouard-Montpetit\, Local M
 -415\, Montréal\, QC\, Canada
SUMMARY:Séminaire Charlie Fehl - University of Oxford
DESCRIPTION:Titre :GT-Predict: Rationalizing a complete family of glycosylt
 ransferase biocatalysts using cheminformatics -and-  Photoredox chemistr
 y for catalytic\, site-selective protein modificationEndroit : Pavillon Ro
 ger-Gaudry\, salle G-815 à 11 h 30.
\nCette conférence sera prononc
 ée par Charlie Fehl\, Ph.D. de l'Université d'Oxford.
\nRésumé :I ut
 ilize chemical insight and techniques to approach biochemical problems at 
 atomic resolution. A current challenge in the age of genomic datasets is c
 hemically-detailed functional prediction\, especially in large protein fam
 ilies where sequence alignment cannot offer the precision to predict which
  small molecules will act as substrates for a particular enzyme family mem
 ber. To develop such a predictive system\, we combine functional profiling
  of a full set of glycosyltransferase family 1 (GT1) enzymes from a single
  species with data mining approaches. Our resultant informatics strategy\,
  “GT-Predict\,” was able to predict enzyme activity for small molecule
  substrates with high accuracy and quality. Coupling this cheminformatic d
 ataset with local sequence alignment further enabled functional prediction
  (i.e. of substrate scope) for new GT enzymes from amino acid sequence alo
 ne. Finally\, key residues for substrate recognition and activity were hig
 hlighted and confirmed using mutagenesis. We seek to apply this strategy t
 o streamline the use and design of biocatalysts\, as well as enabling chem
 ically-detailed functional annotation of genomic datasets.
\nA very differ
 ent challenge in protein biochemistry lies in the synthesis of post-transl
 ationally modified species. Building on radical addition chemistry to forg
 e C-C bonds\, I have developed a protein-compatible photoredox activation 
 manifold for the installation of a variety of custom amino acid sidechains
 . We utilize the site selectivity of the readily-installed dehydroalanine 
 modification as a radical acceptor. By taking advantage of the full range 
 of redox capabilities of water-soluble Ruthenium and Iridium photocatalyst
 s\, I developed conditions to generate radicals via reduction of alkyl hal
 ide as well as oxidation of alkyl boronic acid species. This enables the e
 fficient functionalization of proteins with a variety of natural and unnat
 ural amino acids as well as several post-translational modifications for c
 hemically-defined biological studies.
\nAffiche de la conférence
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