title: Chemical, thermal, and electric field induced unfolding of single protein molecules studied using nanopores.
abstract: Single-molecule experimental techniques have recently shown to be of significant interest for use in numerous applications in both the research laboratory and industrial settings. Although many single-molecule techniques exist, the nanopore platform is perhaps one of the more popular techniques due to its ability to act as a molecular sensor of biological macromolecules. For example, nanopores offer a unique, new method for probing various properties of proteins and can contribute to elucidating key biophysical information in conjunction with existing techniques. In the present study, various forms of bovine serum albumin (BSA) are detected including thermally refolded BSA, urea-denatured BSA, and multiple forms of BSA detected at elevated electric field strengths (with and without urea). We also provide excluded volume measurements for each of these states that normally are difficult to obtain due to unknown and unstable protein conformations.
authors: Department of Chemical and Biological Engineering, Drexel University, Philadelphia, Pennsylvania 19104, USA.
authors: Kevin J
authors: KJ
authors: Freedman
authors: Maike
authors: M
authors: Jürgens
authors: Anmiv
authors: A
authors: Prabhu
authors: Chi Won
authors: CW
authors: Ahn
authors: Per
authors: P
authors: Jemth
authors: Joshua B
authors: JB
authors: Edel
authors: Min Jun
authors: MJ
authors: Kim