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SUMMARY:Fuzziness in function and evolution of proteins - Dr Monika Fuxrei
 ter\, MTA-DE Momentum Laboratory of Protein Dynamics\, Department of Bioch
 emistry and Molecular Biology\, University of Debrecen\, Hungary
DTSTART:20170322T103000Z
DTEND:20170322T113000Z
UID:TALK71442@talks.cam.ac.uk
CONTACT:Priyanka Joshi
DESCRIPTION:Proteins are traditionally described by a deterministic relati
 onship between the sequence\, structure and function. The recognition of p
 rotein dynamics is increasing\, the ambiguities in conformations and inter
 action patterns however\, are still largely ignored. The structural multip
 licity or dynamic disorder in protein complexes that contributes to regula
 ted formation or function of the assemblies is referred to as fuzziness. A
 ccumulating experimental evidence corroborates the importance of fuzziness
  in a variety of protein organizations and a wide spectrum of activities r
 anging from enzymatic catalysis to regulatory machines. Fuzzy regions coul
 d serve as transient interaction elements to mediate direct contacts or in
 fluence adjacent binding interfaces\, as well as play a role as largely un
 structured linkers and tails that may connect separate binding modules to 
 increase their local concentration. Conformational diversity within protei
 n complexes and higher-order assemblies results in a variety of regulatory
  pathways\, including promoting/relieving intramolecular autoinhibition\, 
 facilitating allostery\, or responding to posttranslational modifications 
 via well-characterized mechanisms (see FuzDB: http://protdyn-database.org)
 . I will provide an overview of how fuzziness interferes with existing and
  newly evolving protein functions. \n
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
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