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UID:20260304T183913EST-3758FOJCxR@132.216.98.100
DTSTAMP:20260304T233913Z
DESCRIPTION:Abstract:\n\nMulticellular life is scaffolded by structures tha
 t maintain cells in the desired locations and organizations. The collagen 
 family of proteins has been selected via evolution as the preferred buildi
 ng block of these extracellular structures\, yet surprisingly\, collagen p
 roteins are structurally unstable at body temperature.\n\nIn this talk\, I
  will introduce some of the fascinating physical properties of the unique 
 triple-helix structure of collagen\, and will highlight the results of our
  investigations into the sequence dependence of its mechanics and stabilit
 y. Our single-molecule approaches include centrifuge force microscopy\, op
 tical tweezers and atomic force microscopy. Our work is revealing clues as
  to how stability is encoded within collagen’s sequence\, and how collagen
 ’s triple helix balances structural stability with responsiveness to appli
 ed force and chemical environment.\n\n \n
DTSTART:20211102T170000Z
DTEND:20211102T183000Z
LOCATION:Zoom link: https://mcgill.zoom.us/j/87946025591?pwd=c0lVdWU4dDN0eX
 E3NFI1Y1FuenRXZz09
SUMMARY:Chemical Society Seminar: Nancy R. Forde - Mechanical properties of
  our unstable protein building blocks
URL:/chemistry/channels/event/chemical-society-seminar
 -nancy-r-forde-mechanical-properties-our-unstable-protein-building-blocks-
 333767
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