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SUMMARY:How fast folding proteins fold - Prof. Kresten Lindorff-Larsen\, U
 niversity of Copenhagen
DTSTART:20111123T141500Z
DTEND:20111123T151500Z
UID:TALK32426@talks.cam.ac.uk
CONTACT:Robert Best
DESCRIPTION:Molecular dynamics simulations provide a vehicle for capturing
  the structures\, motions\, and interactions of biological macromolecules 
 in full atomic detail.  We have performed a systematic and extensive evalu
 ation of a number of different protein force fields based on comparisons o
 f experimental data with molecular dynamics simulations. We then selected 
 one of the most recent and accurate force fields to perform molecular dyna
 mics simulations (over periods ranging between 100 µs and 1 ms) of the fo
 lding of 12 structurally diverse proteins. In the simulations\, the protei
 ns\, representing all three major structural classes\, spontaneously and r
 epeatedly folded to their experimentally determined native structures.  I 
 will present the results of the analyses we performed to identify the comm
 on principles that underlie the folding of these proteins.  We found that 
 early in the folding process\, the protein backbone adopts a native-like t
 opology while certain secondary structure elements and a small number of n
 on-local contacts form.  In most cases\, folding follows a single dominant
  route\, in which elements of the native structure appear in an order high
 ly correlated with their propensity to form in the unfolded state.\n
LOCATION:Department of Chemistry\, Cambridge\, Pfizer lecture theatre
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