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SUMMARY:Comparative studies of intrinsically disordered proteins - Profess
 or Jane Clarke\, Department of Chemistry\, University of Cambridge 
DTSTART:20170123T110000Z
DTEND:20170123T120000Z
UID:TALK70279@talks.cam.ac.uk
CONTACT:Scientific Meetings Co-ordinator
DESCRIPTION:In my laboratory we use a multidisciplinary approach to study 
 protein folding -  how the linear sequence of amino acids in a polypeptide
  chain determines the structure to which it folds\, the pathway by which i
 t folds\, and how it avoids misfolding. That is\, how the primary sequence
  defines the entire energy landscape for folding.\n\nIt has recently becom
 e apparent that many proteins are not\, in fact folded\, but they play imp
 ortant roles in the cell.  These intrinsically disordered protein challeng
 e the structure : function paradigm\, and they have attracted significant 
 interest from investigators in the fields of structural biology\, bioinfor
 matics and theory\, but\, relatively little work has been done using stand
 ard biophysical kinetics techniques pioneered in studies of protein foldin
 g\n\nMany key protein-protein interactions are driven by assembly of compl
 exes where one or both partner proteins are intrinsically disordered befor
 e binding.  In this case the free energy of binding has to compensate for 
 the energetic cost of folding.   We are comparing the folding of a number 
 of different folding-upon binding systems to ask some fundamental question
 s about the mechanisms of folding upon binding: What is the importance of 
 residual structure? What role does the ordered partner play? What is the m
 echanism of assembly? And\, perhaps most fundamentally – what is the fun
 ction of disorder? I will describe some of our recent findings.\n
LOCATION:Max Perutz Lecture Theatre\, Medical Research Council (MRC) (MRC 
 Laboratory of Molecular Biol
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