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DTSTAMP:20260316T120328
DTSTART;TZID=America/Detroit:20260206T120000
DTEND;TZID=America/Detroit:20260206T140000
SUMMARY:Careers / Jobs:LSA Internship Scholarship Office Hours
DESCRIPTION:Do you have questions about the LSA Internship Scholarship? Drop in during our virtual office hours! Whether you need help with your application or have any other questions\, we’re here to help. Pop into our Zoom session at a time that works for you. These drop-in style office hours are designed for students who have questions regarding the LSA Internship Scholarship Application or internship eligibility requirements.\n\nClick the link in the side bar for your timeslot today! Be sure to toggle to 1/9/2026.\nThe final deadline for the scholarship is April 15!\n\nCan't make it? Check out our other dates below: \nJanuary 23rd\nFebruary 6th\nFebruary 27th\nMarch 13th\nMarch 27th\nApril 10th
UID:142414-21891731@events.umich.edu
URL:https://events.umich.edu/event/142414
CLASS:PUBLIC
STATUS:CONFIRMED
CATEGORIES:Career,Internship,Lsa Opportunity Hub
LOCATION:Off Campus Location
CONTACT:
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DTSTAMP:20260121T141433
DTSTART;TZID=America/Detroit:20260206T120000
DTEND;TZID=America/Detroit:20260206T130000
SUMMARY:Workshop / Seminar:Membrane Protein Folding: What Lipids Do?
DESCRIPTION:My talk addresses two questions regarding how the lipid bilayer environment in cells mediates folding and function of membrane proteins: 1) Is the lipid bilayer a good solvent for the denatured states of membrane proteins? 2) What is the role of lipid solvation in the stability and cooperativity of membrane proteins? We have developed an array of “steric trapping”-based methods to delineate the thermodynamic stability\, conformational features of the denatured states\, and residue interaction network of membrane proteins. Using the intramembrane protease GlpG of E. coli as a model\, we find that the bilayer environment 1) induces contraction but not collapse of the denatured state of GlpG\, 2) enhances the stability of the protein by facilitating the residue burial in the protein interior\, and 3) strengthens the residue-interaction network such that the whole residue-packed regions can act as a single cooperative unit. I will discuss how these properties shed light and cast shadows on the folding\, quality control\, and function of membrane proteins.
UID:144264-21895048@events.umich.edu
URL:https://events.umich.edu/event/144264
CLASS:PUBLIC
STATUS:CONFIRMED
CATEGORIES:Biophysics
LOCATION:Chemistry Dow Lab - 1640
CONTACT:
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