Literature Seminar:

Ultrafast laser spectroscopy can allow for the dynamics of biological systems to be investigated in ways not possible through other methods. Understanding the time-resolved dynamics of protein systems can more precisely elucidate the mechanisms that drive protein structure and function. Crystallins, are a class of proteins that predominantly form the cornea of the eye in all vertebrates. Crystallins must remain hydrated throughout the duration of a vertebrate’s life for vision to persist. When crystallin proteins lose their solubility, they aggregate and form cloudy regions in the cornea that are known as cataracts. Using femtosecond fluorescence upconversion spectroscopy in combination with site-directed tryptophanyl mutagenesis, the dynamics of specific regions in crystallin proteins can be probed. Information on site-specific hydration 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 medical community as cataracts are estimated to develop within 50 % of individuals by the age of 75. More broadly, these studies serve as a model for how site-specific protein dynamics can be investigated with ultrafast laser spectroscopy.