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SUMMARY:Molecular origins of &quot\;internal friction&quot\; in protein fo
 lding - Dr. David de Sancho\, Department of Chemistry\, University of Camb
 ridge
DTSTART:20140613T110000Z
DTEND:20140613T120000Z
UID:TALK52809@talks.cam.ac.uk
CONTACT:Dr. Judith B. Rommel
DESCRIPTION:Protein dynamics are influenced by solvent friction\, due to t
 he \ncollisions of the sorrounding water molecules. However\, another type
 \nof friction\, emerging from the interactions of the polypeptide chain\n 
 with itself\, has also been found to be prevalent in protein and \npeptide
  folding\, unfolded state dynamics and disordered proteins.\nHowever a cle
 ar molecular interpretation of this phenomenon is still\nmissing. Here we 
 examine this contribution using atomistic molecular \ndynamics simulations
  of several small proteins and peptides and model \nsystems. We find that 
 the experimental signatures usually attributed to \ninternal friction can 
 emerge from the features of protein energy landscapes. In particular the c
 rossing of sharp torsional barriers\, which are ubiquitous in protein conf
 ormational transitions\, are sufficient to explain the anomalous viscosity
  dependence observed in experiments for  many different systems\, without 
 the need to invoke an  "internal"  frictional effect.\n
LOCATION:Unilever Lecture Theatre\, Department of Chemistry
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