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UID:438@biocityturku.fi
DTSTART;TZID=Europe/Helsinki:20191114T120000
DTEND;TZID=Europe/Helsinki:20191114T130000
DTSTAMP:20231013T063133Z
URL:https://biocityturku.fi/events/frontiers-of-science-membrane-protein-i
 nteractions-and-function-viewed-by-molecular-simulations/
SUMMARY:Frontiers of Science: Membrane protein interactions and function vi
 ewed by molecular simulations
DESCRIPTION:Prof. Mark Sansom\, Department of Biochemistry\, University of 
 Oxford\, UK\nMembrane protein interactions and function viewed by molecula
 r simulations\n\nHost: Parthiban Marimuthu (Parthiban.Marimuthu@abo.fi)\n\
 nMark Sansom heads a group of 20 researchers focusing on biomolecular simu
 lations of membranes. Current topics of research include membrane protein/
 lipid interactions\, and the behaviour of water in ion channels and nanopo
 res. He has worked for over 25 years at the interface between life and phy
 sical sciences\, and has ca. 550 500 publications with an h index of 80. H
 e has also played a role in helping to develop UK HPC strategy.\n\nSelecte
 d recent papers\nRao\, S.\, Klesse\, G.\, Stansfeld\, P.J.\, Tucker\, S.J.
 \, &amp\; Sansom\, M.S.P. (2019) A heuristic derived from analysis of the 
 ion channel structural proteome permits the rapid identification of hydrop
 hobic gates. PNAS 116: 13989-13995.\n\nSaotome\, K.\, Teng\, T.\, Tsui\, C
 .C. (A.)\, Lee\, W.H.\, Sansom\, M.S.P.\, Liman\, E.R. &amp\; Ward\, A.B. 
 (2019) Structures of the otopetrin proton channels Otop1 and Otop3. Nature
  Struct. Molec. Biol. 26: 518–525.\n\nSong\, W.\, Yen\, H.-Y.\, Robinson
 \, C.V.\, &amp\; Sansom\, M.S.P. (2019) State-dependent lipid interactions
  with the A2a receptor revealed by MD simulations using in vivo-mimetic me
 mbranes. Structure 27: 392–403.\n\nYen\, H.-Y.\, Hoi\, K.K.\, Liko\, I.\
 , Hedger\, G.\, Horrell\, M.R.\, Song. W.\, Wu\, D.\, Heine\, P.\, Warne\,
  T.\, Lee\, Y.\, Carpenter\, B.\, Plückthun\, A.\, Tate\, C.G.\, Sansom\,
  M.S.P. &amp\; Robinson\, C.V. (2018) PtdIns(4\,5)P2 stabilises active sta
 tes of GPCRs and enhances selectivity of G-protein coupling. Nature 559: 4
 23–427.
CATEGORIES:BiocityTurku events
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