Probing protein nanopores with poly(ethylene glycol)s. Issue 5 (24th January 2022)

• Record Type: Journal Article
• Authors: Liu, Wenxing; Nestorovich, Ekaterina M.
• Editors: Robertson, Joseph W. F.; Reiner, Joseph E.
• Is Part Of: Proteomics. Volume 22:Issue 5/6(2022)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2022-01-24
• Subjects: channel sizing -- current noise analysis -- PEG partitioning -- polymer/pore interaction -- polymer transport; Proteins -- Separation -- Periodicals; Bioinformatics -- Periodicals; Proteomics -- Periodicals; Genomes -- Periodicals; Molecular genetics -- Periodicals; 572.605
• DOI: 10.1002/pmic.202100055
• Languages: English
• ISSNs: 1615-9853

Abstract

Abstract: Neutral water‐soluble poly(ethylene glycol)s (PEGs) have been extensively explored in protein nanopore research for the past several decades. The principal use of PEGs is to investigate the membrane protein ion channel physical characteristics and transport properties. In addition, protein nanopores are used to study polymer–protein interactions and polymer physicochemical properties. In this review, we focus on the biophysical studies on probing protein ion channels with PEGs, specifically on nanopore sizing by PEG partitioning. We discuss the fluctuation analysis of ion channel currents in response to the PEGs moving within their confined geometries. The advantages, limitations, and recent developments of the approach are also addressed.