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SUMMARY:Membrane Protein Structures and Ligand Binding From Solid-State NM
 R
DTSTART:20181025T171500
DTEND:20181025T181500
DTSTAMP:20260415T235905Z
UID:badc0855fac35cbcbc65b556cd28c4becd420a263b3f63480b900ce1
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Mei Hong\nMIT\, Departement of chemistry\nUSA\nMembrane 
 proteins carry out a myriad of cellular functions such as ion conduction\,
  metabolite transport\, and signaling. Solid-state NMR spectroscopy allows
  us to obtain detailed atomic information of membrane protein structures a
 nd dynamics that underlie these functions. I will present our investigatio
 ns of the structure and dynamics of two viral membrane proteins. The influ
 enza virus M2 protein transports protons across the viral lipid envelope a
 nd conducts membrane scission. We have not only characterized the structur
 al dynamics that underlies proton transport\, but also determined how chol
 esterol binds M2 to mediate membrane scission. The cholesterol-bound prote
 in structure gave unexpected insight into how M2 is attracted to the neck 
 of the budding virus to cause membrane curvature. In a second study\, we h
 ave determined the structure and assembly of the C-terminal membrane-assoc
 iated region of the HIV fusion protein\, gp41. Both these studies extensiv
 ely employ 19F NMR of fluorinated protein or ligand. Fluorine is a high-s
 ensitivity nuclear spin with many favorable NMR properties. We have develo
 ped a collection of19F-based NMR techniques for high-field and fast magic-
 angle-spinning conditions\, to measure inter-atomic distances to a much hi
 gher upper limit (~ 2 nm) than possible by13CNMR.
LOCATION:BCH 2201 https://plan.epfl.ch/?room==BCH%202201
STATUS:CONFIRMED
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