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SUMMARY:Increasing functional versatility of proteins by regulated unfoldi
 ng and exposing disordered regions - Dr Rita Pancsa
DTSTART:20161124T131000Z
DTEND:20161124T140000Z
UID:TALK69318@talks.cam.ac.uk
CONTACT:Janet Gibson
DESCRIPTION:Proteins are the fundamental executor molecules of living cell
 s. They are polymers of amino acids and their functioning is tightly linke
 d with their structure\, i.e. the precise positioning of atoms. Recently\,
  it has been shown that proteins may remain unstructured/disordered and ye
 t be functional. More excitingly\, certain proteins can interconvert betwe
 en different folded structures and undergo a change between folded and uns
 tructured conformations in a controlled and reversible manner (Regulated U
 nfolding\; RU). In certain cases whole protein domains unfold as a result 
 of minor chemical modifications\, so called post-translational modificatio
 ns (PTMs)\, exposing cryptic disordered segments affecting both protein ce
 llular localization and interactions. Thus a fundamental open question is 
 how prevalent is regulated unfolding and what are the underlying molecular
  principles?\nWe hypothesize that RU is widely prevalent\, because by cond
 itionally exposing disordered regions hosting short linear interaction mot
 ifs (SLiMs) reversible conformational changes could alter the cellular loc
 alization and interactions of proteins and provide increased functional pl
 asticity during conditions such as stress. The reason why RU remained unde
 rstudied so far is most probably the lack of structural information for mo
 dified proteins.\nWe develop and apply an inter-disciplinary computational
  and experimental approach involving the targeted discovery and characteri
 zation of proteins undergoing RU to elucidate the prevalence and biologica
 l relevance. Introducing regulated unfolding as a novel layer of protein f
 unction regulation will lay the foundations of a novel concept in biology.
 \n
LOCATION:The Richard King Room\, Darwin College
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