Translational mobilities of proteins in nanochannels: A coarse-grained molecular dynamics study

Haridasan, N, Kannam, S, Mogurampelly, S and Sathian, S 2018, 'Translational mobilities of proteins in nanochannels: A coarse-grained molecular dynamics study', Physical Review E, vol. 97, no. 6, pp. 1-7.


Document type: Journal Article
Collection: Journal Articles

Title Translational mobilities of proteins in nanochannels: A coarse-grained molecular dynamics study
Author(s) Haridasan, N
Kannam, S
Mogurampelly, S
Sathian, S
Year 2018
Journal name Physical Review E
Volume number 97
Issue number 6
Start page 1
End page 7
Total pages 7
Publisher American Physical Society
Abstract We investigated the translation of a protein through model nanopores using coarse-grained (CG) nonequilibrium molecular dynamics (NEMD) simulations and compared the mobilities with those obtained from previous coarse-grained equilibrium molecular dynamics model. We considered the effects of nanopore confinement and external force on the translation of streptavidin through nanopores of dimensions representative of experiments. As the nanopore radius approaches the protein hydrodynamic radius, rh/rp?1 (where rh is the hydrodynamic radius of protein and rp is the pore radius), the translation times are observed to increase by two orders of magnitude. The translation times are found to be in good agreement with the one-dimensional biased diffusion model. The results presented in this paper provide useful insights on nanopore designs intended to control the motion of biomolecules.
Subject Mathematical Sciences not elsewhere classified
Physical Sciences not elsewhere classified
Engineering not elsewhere classified
Keyword(s) solid-state nanopores
polymer translocation
DNA translocation
single
transport
channel
simulations
membrane
pore
electrophoresis
DOI - identifier 10.1103/PhysRevE.97.062415
Copyright notice © 2018 American Physical Society.
ISSN 2470-0045
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 3 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 0 times in Scopus Article
Altmetric details:
Access Statistics: 2 Abstract Views  -  Detailed Statistics
Created: Thu, 23 May 2019, 08:44:00 EST by Catalyst Administrator
© 2014 RMIT Research Repository • Powered by Fez SoftwareContact us