Directional conformer exchange in dihydrofolate reductase revealed by single-molecule nanopore recordings
Abstract
Conformational heterogeneity is emerging as a defining characteristic of enzyme function. However, understanding the role of protein conformations requires their thermodynamic and kinetic characterization at the single-molecule level, which remains extremely challenging. Here we report the ligand-induced conformational changes of dihydrofolate reductase (DHFR) by measuring the modulation of the nanopore currents. The long observation time of the...
Paper Details
Title
Directional conformer exchange in dihydrofolate reductase revealed by single-molecule nanopore recordings
Published Date
Apr 6, 2020
Journal
Volume
12
Issue
5
Pages
481 - 488
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