Structural and functional consequences of age-related isomerization in α-crystallins

Yana A. Lyon

Current position: Research Scientist, Gilead Sciences, Oceanside, California

Education: Ph.D. in Analytical Chemistry, 2018, University of California, Riverside, California

Where to find me: https://www.linkedin.com/in/yana-lyon-461a93a5

How did you become interested in this topic?

My interest in understanding the structural consequences of isomerization and its role in aging and disease began when we mapped out the isomerization profiles between the water-soluble and water-insoluble fractions of both animal and human lenses. Some regions in the crystallin proteins showed a high degree of isomerization in the insoluble fraction and a lack thereof in the soluble. This spurred our curiosity and set the framework for the structural and functional consequences we mapped out in this manuscript.

Can you describe an exciting moment you experienced while doing this research?

When we got the initial native mass spectrometry data from the Benesch group showing that the D-serine version of the C-terminal peptide did not bind to the core domain, we were ecstatic. It was incredible to see how they were able to use such a delicate ionization method to show how the stereoinversion of a single amino acid can have such a large impact on binding.

Where do you seek scientific inspiration?

I seek scientific inspiration at conferences. I enjoy seeing the incredible work being done by my peers, the breakthroughs and new technologies being discovered, and the opportunity to present my research and get critical feedback from others.

Read Lyon's article on page 7546.

This Article

  1. JBC May 10, 2019 vol. 294 no. 19 7546-7555
  1. Free via Open Access: OA
  2. Supporting Information
  3. Author profile: Miranda P. Collier
  4. ? Author profile: Yana A. Lyon

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