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UID:DSC-19486
DTSTART;TZID=Europe/Berlin:20230131T150000
SEQUENCE:1675233407
TRANSP:OPAQUE
DTEND;TZID=Europe/Berlin:20230131T160000
URL:https://www.dresden-science-calendar.de/calendar/de/detail/19486
LOCATION:MPI-CBG\, Pfotenhauerstraße 10801307 Dresden
SUMMARY:Sartori: Structure\, function\, and evolutionary conservation in AT
 P synthase
CLASS:PUBLIC
DESCRIPTION:Speaker: Pablo Sartori\nInstitute of Speaker: IGC\, Portugal\nT
 opics:\n\n Location:\n  Name: MPI-CBG (CSBD SR Top Floor)\n  Street: Pfote
 nhauerstraße 108\n  City: 01307 Dresden\n  Phone: +49 351 210-0\n  Fax: +
 49 351 210-2000\nDescription: One of the tenets of molecular biology is th
 at dynamical transitions between three dimensional structures largely dete
 rmine the function of proteins. Therefore\, it seems only natural that evo
 lutionary analysis of proteins\, presently based on their primary sequence
 \, needs to shift its focus towardsprotein function\, as assessed by corre
 sponding structural transitions.  We will show how to adapt the formalism 
 of finite strain analysis\, developed in condensed matter physics and engi
 neering\, and apply it to structural transitions of proteins. As a case st
 udy\, we will focus on the ATP synthase\, for which our Protein Strain Ana
 lysis (PSA) provides a strain distribution on the protein structure associ
 ated with functional transitions. By analyzing the strain patterns for ATP
  synthases across different species\, we show that they are evolutionarily
  conserved for the same functional transition. This observed strain conser
 vation across evolutionary distant species indicates that this quantity sh
 ould be essential in future structure-based evolutionary studies of protei
 n function.
DTSTAMP:20260905T063830Z
CREATED:20230127T063847Z
LAST-MODIFIED:20230201T063647Z
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