Since 1987, I have been working in vision research investigating both the proteostasis and the proteomics of the lens. While a post-doctoral fellow with Dr. Larry David, I identified deamidation as the major post-translational modification of proteins in the human lens during aging and cataract formation. Together Dr. David and I have a longstanding collaboration to determine the role of deamidation in protein dynamics using multiangle laser scattering and high-resolution mass spectrometry.

I have focused my laboratory on the role of the deamidation in β/g-crystallin structure and function and protein-protein interactions. Deamidation, which introduces a negative charge in a protein, decreases the stability of the crystallins, increases their propensity to aggregate and to escape rescue by the protective α-crystallin chaperone. We have applied the highly sensitive methods of static and dynamic light scattering to determine soluble aggregate sizes and hydrogen-deuterium exchange with high-resolution mass spectrometry to identify subtle structural changes.  We have used these methods to determine that β-crystallins are flexible and take on different conformations depending on the partner subunit, representing a fundamental change in how we view these structural proteins.  Our goal is to understand the native interactions in the lens in order to increase the protective stabilizing interactions disrupted by deamidation. 

For additional information:  http://www.ncbi.nlm.nih.gov/sites/myncbi/kirsten.lampi.1/bibliograpahy/40349583/public/?sort=date&direction=descending