babyÖ±²¥app

B.S. in Chemistry, babyÖ±²¥app School of Mines

NIH Molecular Biophysics Trainee (2013-2015)

Telomere Biology, Plasticity in Recognition, Non-Canonical RNA Function

I am broadly interested in protein-nucleic acid specificity and the structure-function relationships of these interactions. The single-stranded DNA binding protein, Pot1, which binds to and protects telomeres shows remarkable plasticity at the protein-nucleic acid interface. In S. pombe Pot1, substitution in the telomere sequence results in alternative binding modes, with some substitutions resulting is large structural rearrangements in both protein and ligand without loss of affinity. Stunningly, these same structural rearrangements in the presence of base substitutions are utilized by the protein to discriminate against the much smaller hydroxyl substitutions in RNA of the same sequence.

In addition, recent crosslinking studies have implicated a large population of proteins that bind RNA without any known RNA-binding domains, and I am interested in determining the mechanism by which select proteins from these studies are involved in RNA biology.

Other interests: Outside lab, Neil likes to play board games, read, and hike.