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BEGIN:VEVENT
DTSTAMP:20260408T163013Z
DTSTART;VALUE=DATE-TIME:20231115T130000
DTEND;VALUE=DATE-TIME:20231115T140000
SUMMARY:BMS Seminar: In situ structures of muscle sarcomere and sarcomeri
 c proteins\, Professor Stefan Raunser\, Department of Structural Biochem
 istry\, Max Planck Institute of Molecular Physiology\, Germany
TZID:Europe/London
UID:20231115-8a1785d7898c299401899c9a1afa3d4a@warwick.ac.uk
CREATED:20231110T120546Z
DESCRIPTION:Abstract: Sarcomeres are force-generating and load-bearing de
 vices of muscles. A precise molecular picture of how sarcomeres are buil
 t underpins understanding their role in health and diseases. We determin
 ed the molecular architecture of native skeletal and cardiac sarcomeres 
 and structures of sarcomeric proteins using cryo-focused-ion-beam millin
 g (cryo-FIB) and electron cryo-tomography (cryo-ET). Our three-dimension
 al reconstruction of the sarcomere reveals molecular details in the A-ba
 nd\, I-band and Z-disc and demonstrates the organisation of the thin and
  thick filaments and their cross-links [1\,2]. Our reconstruction of the
  thick filament reveals the three-dimensional organization of myosin hea
 ds and tails\, myosin-binding protein C (MyBP-C) and titin\, elucidating
  the structural basis for their interaction during muscle contraction [2
 ]. Using sub-tomogram averaging\, we determined an in situ structure of 
 a nebulous thin-filament-binding protein\, nebulin\, at 4.5 Å and demons
 trated the molecular mechanism underlying its role as a "molecular ruler
 "\, in stabilising thin filament and in regulating myosin binding [3]. W
 e also characterised the structure of a unique double-head myosin confor
 mation\, highlighting the inherent structural variability of myosin in m
 uscle [1]. References: [1] Wang\, Z\, Grange M et al. (2021)\, Cell. 184
 \,2135-2150.613 [2] Tamborrini\, D et al. (2023)\, bioRxiv\, https://doi
 .org/10.1101/2023.04.11.536387 [3] Wang\, Z\, Grange M et al. (2022)\, S
 cience. 375\, eabn1934 doi: 10.1126/science.abn1934 Biography: Professor
  Stefan Raunser is a structural biologist whose research focuses on unde
 rstanding molecular mechanisms underlying cellular processes in the heal
 thy and diseased organism. He is Director of the Department of Structura
 l Biochemistry at the Max Planck institute of Molecular Physiology\, Adj
 unct Professor at Technical University Dortmund and Honorary Professor a
 t University of Duisburg-Essen. With his research group\, he uses a mult
 i-disciplinary approach\, including biochemical reconstitutions\, high-r
 esolution electron cryomicroscopy (cryo-EM) and electron cryotomography 
 (cryo-ET) primarily to investigate the structure of macromolecular compl
 exes that play a crucial role in cell physiology\, with a particular emp
 hasis on toxin-mediated membrane permeation\, the molecular details of m
 uscle contraction and the dynamics of the eukaryotic cytoskeleton. A det
 ailed understanding of these processes is of great importance as they ul
 timately serve to develop pharmaceutical measures to combat disease. He 
 has authored over 100 papers in the fields of structural and molecular b
 iology and has given over 200 lectures and seminars around the world. He
  is a scientific member of the Max Planck Society and an elected member 
 of the North Rhine Westphalian Academy of Sciences and Arts\, the German
  National Academy of Sciences Leopoldina and EMBO.
LOCATION:IBRB Lecture Theatre
CATEGORIES:BiomedicalSciences,DivisionalSeminars
LAST-MODIFIED:20231110T120546Z
ORGANIZER;CN=Jas Bains:
END:VEVENT
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