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DTSTART;TZID=America/Toronto:20240409T080000
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CREATED:20250314T182827Z
LAST-MODIFIED:20260604T155033Z
UID:1044-1712649600-1712682000@mycrbi.com
SUMMARY:CRBI/CIRC Seminar
DESCRIPTION:CRBI/CIRC Seminar – Dr. Derek Wilson\, Professor Department of Chemistry \nUnderstanding COVID vaccine efficacy on the molecular level
URL:https://mycrbi.com/event/1044/
CATEGORIES:Seminars
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BEGIN:VEVENT
DTSTART;TZID=America/Toronto:20240423T103000
DTEND;TZID=America/Toronto:20240423T120000
DTSTAMP:20260623T233904
CREATED:20250314T183010Z
LAST-MODIFIED:20260604T155029Z
UID:1046-1713868200-1713873600@mycrbi.com
SUMMARY:CRBI/CIRC Seminar
DESCRIPTION:CRBI/CIRC Seminar – Dr. Sebastian Magierowski\, Associate Professor\, Dept of Electrical Engineering & Computer Science York University \nSequencing on Silicon
URL:https://mycrbi.com/event/1046/
CATEGORIES:Seminars
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BEGIN:VEVENT
DTSTART;TZID=America/Toronto:20240425T133000
DTEND;TZID=America/Toronto:20240425T143000
DTSTAMP:20260623T233904
CREATED:20250312T184836Z
LAST-MODIFIED:20260604T155025Z
UID:985-1714051800-1714055400@mycrbi.com
SUMMARY:CRBI/CIRC Seminar
DESCRIPTION:CRBI Seminar – Dr. Martin Schmeing\, McGill University Thursday April 25th 2024 \nBiosynthesis and use of the most interesting polymer you didn’t know existed \nAbstract: \n \nCyanophycin is a natural product polymer with a poly-aspartate backbone and arginines linked to each Asp side chain. Used in bacteria for storage of fixed nitrogen\, carbon and energy\, long chains of cyanophycin coalesce into inert\, membrane-less granules which can occupy most of the volume of a cell. Cyanophycin has a variety of potential green industrial and biomedical applications. Cyanophycin is made by cyanophycin synthetase 1 or 2 through ATP-dependent polymerization of Asp and Arg\, or β-Asp-Arg\, respectively. It is degraded into dipeptides by specialized exo-cyanophycinases\, and these dipeptidase are hydrolyzed into free amino acids by nonspecific isoaspartyl dipeptidases. I will share highlights of our structural and functional studies of cyanophycin biosynthesis and degradation\, which led to surprising discoveries: Our structures and biochemical assays of the cyanophycin synthetase 1 revealed it to be a remarkable\, multi-domain\, multi-functional biosynthetic machine and uncovered a hidden hydrolytic active site that is crucial for rapid biosynthesis. We also showed that cyanophycin synthetase 2 can assume several elegant architectures that influence its synthetic activity. Further\, we discovered and characterized a novel\, large family of isoaspartyl dipeptidases dedicated to cyanophycin metabolism\, which allows the human pathogen Pseudomonas aeruginosa to use β-Asp-Arg as a sole carbon source\, and as good a sole nitrogen source as ammonium. Bioinformatics results underscore how common it is for bacteria to be cyanophycin producers or scavengers\, much more so than currently appreciated. 
URL:https://mycrbi.com/event/985/
CATEGORIES:Seminars
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