Henry S. White received the B.S. degree in chemistry from the University of North Carolina (1978) and the Ph.D. degree in chemistry from the University of Texas (1983). Following a postdoctoral appointment at the Massachusetts Institute of Technology, he joined the faculty of the Department of Chemical Engineering and Materials Science at the University of Minnesota, where he was the McKnight and Shell Professor of Chemical Engineering. In 1993, he moved to Chemistry at the University of Utah. Prof. White is an electrochemist, with interests in biological, physical, and materials chemistry. Current research interests include DNA structural analyses using ion channel recordings, electrochemistry in nanometer-wide cells, the formation and stability of nanobubbles, and ion transport in nanopores. He is a Fellow of the American Academy of Arts and Sciences and is the recipient of the Faraday Medal of the Royal Society of Chemistry, the Reilley Award of the Society of Electroanalytical Chemistry, the Grahame Award of the Electrochemical Society, and the ACS Analytical Division Award in Electrochemistry.
Application of the Latch Sensing Zone in a-Hemolysin for Analysis of ds-DNA
Friday, 19 September 2014 at 15:30
Add to Calendar ▼2014-09-19 15:30:002014-09-19 16:30:00Europe/LondonApplication of the Latch Sensing Zone in a-Hemolysin for Analysis of ds-DNALab-on-a-Chip, Microfluidics and Microarray World Congress in San Diego, California, USASan Diego, California, USASELECTBIOenquiries@selectbiosciences.com
Nanopores have been investigated as a simple and label-free tool to characterize DNA nucleotides when a ssDNA strand translocates through the constriction of the pore. Here, a wild-type a-hemolysin protein nanopore was used to monitor DNA repair enzyme activity based on base-specific interactions of dsDNA with the vestibule constriction “latch”, a previously unrecognized sensing zone in a-hemolysin specific for dsDNA structure. The presence of a single abasic site within dsDNA that is in proximity of the latch zone results in a large increase in ion channel current, allowing accurate quantitation of the kinetics of base repair reactions involving an abasic site product. Taking advantage of the high resolution for abasic site recognition, the rate of uracil-DNA glycosylase hydrolysis of the N-glycosidic bond, converting 2’-deoxyuridine in DNA to an abasic site, was continuously monitored by electrophoretically capturing reaction substrate or product dsDNA in the ion channel vestibule. Our results can be adapted to monitor the activity of other enzymes that introduce a change in the oligonucleotide structure, and thus provide a new approach for monitoring enzymatic activity on DNA. The discovery of a very sensitive sensing zone at the latch suggests the potential development of new methods to detect site-specific changes in dsDNA structure relevant to epigenetic, forensic and medical diagnostic applications.
Authors: Qian Jin, Aaron M. Fleming, Robert P. Johnson, Yun Ding, Cynthia J. Burrows, and Henry S. White
Add to Calendar ▼2014-09-18 00:00:002014-09-19 00:00:00Europe/LondonLab-on-a-Chip, Microfluidics and Microarray World CongressLab-on-a-Chip, Microfluidics and Microarray World Congress in San Diego, California, USASan Diego, California, USASELECTBIOenquiries@selectbiosciences.com
Add to Calendar ▼2014-09-19 15:30:002014-09-19 16:30:00Europe/LondonApplication of the Latch Sensing Zone in a-Hemolysin for Analysis of ds-DNALab-on-a-Chip, Microfluidics and Microarray World Congress in San Diego, California, USASan Diego, California, USASELECTBIOenquiries@selectbiosciences.com
