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SUMMARY:Identification of structure-conserving correlated motions in the 
 β-sheet of ubiquitin - Xavier Salvatella\, Laboratory of Molecular Biophy
 sics\, IRB Barcelona
DTSTART:20090306T141500Z
DTEND:20090306T151500Z
UID:TALK16201@talks.cam.ac.uk
CONTACT:Kevin Chalut
DESCRIPTION:It has been suggested that motions in proteins could be correl
 ated to minimize the net changes to the various energetic contributions th
 at stabilize their native structure. Evidence for motions in proteins has 
 been obtained using molecular dynamics simulations\, Nuclear Magnetic Reso
 nance (NMR)\, fluorescence spectroscopy and single molecule experiments\, 
 but the detection of correlations between the motions of residues distant 
 in sequence has remained an elusive goal due of challenges in directly det
 ermining time-resolved coordinates from experiment. Recently the combinati
 on of NMR data with Molecular Dynamics has been used to characterize prote
 in dynamics at atomic resolution and here we use this approach to probe th
 e dynamics of the protein ubiquitin\; by using the large amount of NMR dat
 a collected on this protein we have generated a large number of conformati
 ons collectively consistent with experiment and validated the resulting en
 semble using independent NMR measurements that average on the same timesca
 le. An analysis of the ensemble reveals that the backbone motions of resid
 ues distant in sequence but connected by hydrogen bonds are correlated and
  provides a pathway for the transfer of structural and dynamical informati
 on across protein structures\, which is the underlying mechanism of bindin
 g allostery and folding cooperativity.
LOCATION:Pippard Lecture Theatre\, Cavendish Laboratory
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