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Chemical, Thermal, and Electric Field Induced Unfolding of Single Protein Molecules Studied Using Nanopores
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
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2011 (English)In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 83, no 13, 5137-5144 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2011. Vol. 83, no 13, 5137-5144 p.
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Medical and Health Sciences
Identifiers
URN: urn:nbn:se:uu:diva-156262DOI: 10.1021/ac2001725ISI: 000292280900018OAI: oai:DiVA.org:uu-156262DiVA: diva2:431234
Available from: 2011-07-18 Created: 2011-07-18 Last updated: 2017-12-08Bibliographically approved

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Jemth, Per

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