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DTSTAMP:20261028T092822Z
UID:68761c4f3b84e068629394@ist.ac.at
DTSTART:20261105T103000
DTEND:20261105T120000
DESCRIPTION:Speaker: Alexandria Deliz Liang\nhosted by Julia Reisenbauer\nA
 bstract: Studying enzyme function or engineering enzymes often relies on m
 utagenesis that enables only coarse-grain modifications that radically cha
 nge the target amino acid. Using genetic code expansion to introduce non-c
 anonical amino acids (ncAAs) can enable atomistic control of mutagenesis. 
 However\, histidine remains challenging to systematically target with this
  method. Histidine has the highest catalytic propensity among canonical am
 ino acids\, enabled by its ability to play versatile roles in catalysis\, 
 including as an acid\, a base\, a nucleophile\, and a coordinating ligand 
 to a catalytic metal. Herein\, we describe a toolkit consisting of nine ne
 w aminoacyl-tRNA synthetase/tRNA pairs for the site-specific genetic encod
 ing of an expanded set of 12 new histidine-like ncAAs. The 12 ncAAs featur
 e broadly tuned nitrogen pKaH\, alternative heterocycles\, and varying sub
 stitution patterns. Herein\, we present the rationale for ncAA selection\,
  the evolution of the toolkit\, and applications of the tool kit to study 
 metalloenzymes.
LOCATION:Office Bldg West / Ground floor / Heinzel Seminar Room (I21.EG.101
 )\, ISTA
ORGANIZER:hcai@ist.ac.at
SUMMARY:Alexandria Deliz Liang: Studying and engineering metalloenzymes thr
 ough genetic code expansion
URL:https://talks-calendar.ista.ac.at/events/5939
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