Single-molecule nanopore enzymology

被引：55

作者：

Willems, Kherim ^{[1
,2
]}

Van Meervelt, Veerle ^{[1
,3
]}

Wloka, Carsten ^{[3
]}

Maglia, Giovanni ^{[3
]}

机构：

[1] Katholieke Univ Leuven, Dept Chem, Celestijnenlaan 200G, B-3001 Leuven, Belgium

[2] IMEC, Dept Life Sci & Imaging, Kapeldreef 75, B-3001 Leuven, Belgium

[3] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Nijenborgh 7, NL-9747 AG Groningen, Netherlands

来源：

PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES | 2017年 / 372卷 / 1726期

基金：

欧洲研究理事会;

关键词：

nanopore enzymology; single-molecule; protein trapping; review; DNA-POLYMERASE COMPLEXES; ALPHA-HEMOLYSIN; PROTEIN TRANSLOCATION; CHAPERONIN CAVITY; ORIGAMI NANOPORES; STRUCTURAL BASIS; STRANDED-DNA; PORE; TRANSPORT; DYNAMICS;

D O I：

10.1098/rstb.2016.0230

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Biological nanopores are a class of membrane proteins that open nanoscale water conduits in biological membranes. When they are reconstituted in artificial membranes and a bias voltage is applied across the membrane, the ionic current passing through individual nanopores can be used to monitor chemical reactions, to recognize individual molecules and, of most interest, to sequence DNA. In addition, a more recent nanopore application is the analysis of single proteins and enzymes. Monitoring enzymatic reactions with nanopores, i.e. nanopore enzymology, has the unique advantage that it allows long-timescale observations of native proteins at the single-molecule level. Here, we describe the approaches and challenges in nanopore enzymology. This article is part of the themed issue 'Membrane pores: from structure and assembly, to medicine and technology'.

引用

页数：11

共 113 条

[1] Imaging α-hemolysin with molecular dynamics:: Ionic conductance, osmotic permeability, and the electrostatic potential map [J].