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SUMMARY:Analysis and interpretation of single molecule force spectroscopy 
 experiments - Brujic\, J (New York University)
DTSTART:20140318T121500Z
DTEND:20140318T125500Z
UID:TALK51486@talks.cam.ac.uk
CONTACT:Mustapha Amrani
DESCRIPTION:Protein unfolding and refolding trajectories under a constant 
 stretching force measure manifestations of the underlying molecular proces
 ses in the end-to-end length fluctuations. In the case of ubiquitin\, I27 
 and NuG2 protein\, the distribution of unfolding times at a given force is
  best fit with a stretched exponential function\, which requires an altern
 ative physical interpretation than the commonly used Kramer's theory. On t
 he other hand\, we show that the collapse from a highly extended state to 
 the folded length is well captured by simple diffusion along the free ener
 gy of the end-to-end length. The estimated diffusion coefficient of ?100nm
 2s?1 is significantly slower than expected from viscous effects alone\, po
 ssibly because of the internal degrees of freedom of the protein. The reco
 nstructed free energy profiles give  validity to a physical model in which
  the multiple protein domains collapse all at once\, independent of the nu
 mber of domains in the in the chain.\n
LOCATION:Seminar Room 1\, Newton Institute
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