@article {270,
	title = {Nanopore Sensing of Protein Folding},
	journal = {ACS Nano},
	volume = {11, 7091-7100},
	year = {2017},
	month = {05/2017},
	abstract = {<p>Single-molecule studies of protein folding\&nbsp;hold keys to unveiling protein folding pathways and elusive intermediate folding states-attractive pharmaceutical targets. Although conventional single-molecule approaches can detect folding intermediates, they presently lack throughput and require elaborate labeling. Here, we theoretically show that measurements of ionic current through a nanopore containing a protein can report on the protein{\textquoteright}s folding state. Our all-atom molecular dynamics (MD) simulations show that the unfolding of a protein lowers the nanopore ionic current, an effect that originates from the reduction of ion mobility in proximity to a protein. Using a theoretical model, we show that the average change in ionic current produced by a folding-unfolding transition is detectable despite the orientational and conformational heterogeneity of the folded and unfolded states. By analyzing millisecond-long all-atom MD simulations of multiple protein transitions, we show that a nanopore ionic current recording can detect folding-unfolding transitions in real time and report on the structure of folding intermediates.</p>
},
	doi = {10.1021/acsnano.7b02718},
	url = {http://pubs.acs.org/doi/abs/10.1021/acsnano.7b02718},
	author = {Si, Wei and Aleksei Aksimentiev}
}
