Cynthia Burrows, Department of Chemistry, University of Utah
Protein Nanopores Reveal Single-Molecule Behavior of DNA & RNA
Self-assembled protein nanopores such as α-hemolysin (α-HL) create a transmembrane channel when inserted into lipid bilayers, and the resulting pore has appropriate dimensions for capture of duplex DNA, DNA hairpins, and G-quadruplexes on the cis side of the pore, while only single-stranded DNA or RNA can translocate through the channel to the trans side under an applied electrophoretic force. We used both WT and site-directed mutants to study the capture of various DNA and RNA secondary structures, with or without base modifications, in a single-molecule analysis. In contrast, Oxford Nanopore Technology has been used to optimize single-molecule sequencing of DNA and RNA strands wherein we have adapted the data analysis to also provide information about the presence of base modifications in, for example, SARS-CoV-2 mRNA.
Curriculum vitae for Cynthia Burrows
Cynthia Burrows is the Thatcher Distinguished Professor of Chemistry at the University of Utah in Salt Lake City. Her studies in organic chemistry at University of Colorado, Cornell University and Université Louis Pasteur, Strasbourg, led eventually to her present interests in the chemistry and biochemistry of modified bases in DNA and RNA with a focus on oxidative stress. This work led to the discovery of an epigenetic role for oxidized DNA bases in G-quadruplex motifs along with new single-molecule methods for understanding nucleic acid folding, the impact of base modifications, and sequencing. Burrows is the recipient of several ACS awards and was inducted into the American Academy of Arts and Sciences in 2009 and to the National Academy of Sciences in 2014. She also serves as Editor-in-Chief of Accounts of Chemical Research.