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SUMMARY:Using Ultrafast Laser Spectroscopy to Investigate Crystallin Protei
 n Dynamics
LOCATION:Chemistry A101
TZID:America/Denver
DTSTART:20211103T160000
UID:2026-05-03-21-39-36@natsci.colostate.edu
DTSTAMP:20260503T213936
Description:Literature Seminar:\n\nUltrafast laser spectroscopy can allow f
 or the dynamics of biological systems to be investigated in ways not possi
 ble through other methods. Understanding the time-resolved dynamics of pro
 tein systems can more precisely elucidate the mechanisms that drive protei
 n structure and function. Crystallins\, are a class of proteins that predo
 minantly form the cornea of the eye in all vertebrates. Crystallins must r
 emain hydrated throughout the duration of a vertebrate’s life for vision
  to persist. When crystallin proteins lose their solubility\, they aggrega
 te and form cloudy regions in the cornea that are known as cataracts. Usin
 g femtosecond fluorescence upconversion spectroscopy in combination with s
 ite-directed tryptophanyl mutagenesis\, the dynamics of specific regions i
 n crystallin proteins can be probed. Information on site-specific hydratio
 n dynamics\, fluorescence anisotropy\, and side-chain motions give insight
  into how crystallin proteins function and remain hydrated in the cornea. 
 These studies have implications that are especially important to the medic
 al community as cataracts are estimated to develop within 50 % of individu
 als by the age of 75. More broadly\, these studies serve as a model for ho
 w site-specific protein dynamics can be investigated with ultrafast laser 
 spectroscopy. 4:00 pm
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