BEGIN:VCALENDAR VERSION:2.0 PRODID:-//Syracuse University Events - ECPv6.0.12//NONSGML v1.0//EN CALSCALE:GREGORIAN METHOD:PUBLISH X-ORIGINAL-URL:https://calendar.syracuse.edu X-WR-CALDESC:Events calendar for the Syracuse University community REFRESH-INTERVAL;VALUE=DURATION:PT1H X-Robots-Tag:noindex X-PUBLISHED-TTL:PT1H BEGIN:VTIMEZONE TZID:America/New_York BEGIN:DAYLIGHT TZOFFSETFROM:-0500 TZOFFSETTO:-0400 TZNAME:EDT DTSTART:20230312T070000 END:DAYLIGHT BEGIN:STANDARD TZOFFSETFROM:-0400 TZOFFSETTO:-0500 TZNAME:EST DTSTART:20231105T060000 END:STANDARD END:VTIMEZONE BEGIN:VEVENT DTSTART;TZID=America/New_York:20230117T160000 DTEND;TZID=America/New_York:20230117T170000 DTSTAMP:20240328T102351 CREATED:20230110T155555Z LAST-MODIFIED:20230110T155555Z UID:87424-1673971200-1673974800@calendar.syracuse.edu SUMMARY:Chemistry Colloquium: Dr. Gabriel Cook DESCRIPTION:The Chemistry Department in the College of Arts and Sciences is pleased to welcome Dr. Gabriel Cook\, an Assistant Professor at Oklahoma State University. \nTitle: In Vitro Glycosylation of Membrane Proteins Involve in Human Disease \nAbstract \nGlycoproteins take part in nearly every biological process and make up a large percent of the proteome. N-glycosyltransferase (NGT) from Actinobacillus pleuropneumoniae\, which recognizes the consensus amino acid sequence\, -Asn-X-Ser/Thr- (NXT) within the protein\, has been shown to successfully glycosylate peptides and proteins in vitro. The enzyme catalyzes glycosidic bond formation between the oligosaccharide donor\, containing nucleoside phosphatase\, and the amide nitrogen of the asparagine residue. We are specifically interested in the properties of membrane glycoproteins\, which are key components in a number of different disease states. In vitro studies of N-linked glycosylation were done in a step-wise fashion in a membrane mimetic environment to confirm the methods for glycosylating soluble proteins could be applicable to membrane proteins. Detergent and lipid systems were used to solubilize the hydrophobic peptides and membrane proteins for glycosylation. Gel electrophoresis\, mass spectrometry\, and NMR studies were used for the detection and quantification of glycosyltransferase activity. Our experiments demonstrated that full-length membrane proteins that contain a N-glycosylation consensus sequence\, can be glycosylated by NGT\, even in the presence of membrane mimetic environments. These methods will be used as the starting point for further oligosaccharide attachment and characterization of structure\, dynamic and interactions of these important proteins. URL:https://calendar.syracuse.edu/events/2023-jan-17/chemistry-colloquium-dr-gabriel-cook/ LOCATION:Center for Science and Technology (CST)\, 1-132 111 College Pl.\, Syracuse\, NY\, 13210\, United States CATEGORIES:Science and Mathematics ATTACH;FMTTYPE=image/jpeg:https://calendar.syracuse.edu/wp-content/uploads/Dr.-Cook-headshot.jpg ORGANIZER;CN="CAS-Department of Chemistry":MAILTO:chemistry@syr.edu GEO:43.0375804;-76.1305763 X-APPLE-STRUCTURED-LOCATION;VALUE=URI;X-ADDRESS=Center for Science and Technology (CST) 1-132 111 College Pl. Syracuse NY 13210 United States;X-APPLE-RADIUS=500;X-TITLE=111 College Pl.:geo:43.0375804,-76.1305763 END:VEVENT END:VCALENDAR