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SUMMARY:Probing protein dynamics by intrinsic tryptophan
DTSTART:20121126T150000
DTEND:20121126T160000
DTSTAMP:20260915T231501Z
UID:de27ab4fd4d7c506e8041b1f577d5087a0f2b1c91996ed70ffa91fb6
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Dongping Zhong\nTryptophan has the longest wavelength ab
 sorption among other amino acids and has recently been used as an optical 
 probe of protein dynamics on ultrafast time scales. Here\, by combing femt
 osecond spectroscopy and site-directed mutagenesis\, we have carried out a
  series of studies including ultrafast protein electron transfer\, resonan
 ce energy transfer\, conformation fluctuations\, and water-protein coupled
  motions\, and observed various nonequilibrium protein dynamics with femto
 second temporal and single-residue spatial resolutions. These studies demo
 nstrated that tryptophan is a powerful molecular probe and can be widely u
 sed for probing ultrafast protein dynamics on the most fundamental level.
LOCATION:CH G1 495 https://plan.epfl.ch/?room==CH%20G1%20495
STATUS:CONFIRMED
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