Translocation intermediates of ubiquitin through an α-hemolysin nanopore: implications for detection of post-translational modifications
Author:
Affiliation:
1. Dipartimento di Ingegneria Meccanica e Aerospaziale Sapienza Università di Roma
2. Roma
3. Italy
4. CNR-Istituto dei Sistemi Complessi UoS Sapienza
5. Dipartimento di Ingegneria Industriale
6. Università di Roma Tor Vergata
Abstract
Molecular dynamics simulations allowed to characterize the co-translocational unfolding pathway of ubiquitin through a biological nanopore.
Publisher
Royal Society of Chemistry (RSC)
Subject
General Materials Science
Link
http://pubs.rsc.org/en/content/articlepdf/2019/NR/C8NR10492A
Reference70 articles.
1. Imaging α-Hemolysin with Molecular Dynamics: Ionic Conductance, Osmotic Permeability, and the Electrostatic Potential Map
2. A Statistical Model for Translocation of Structured Polypeptide Chains through Nanopores
3. Acidity-Mediated, Electrostatic Tuning of Asymmetrically Charged Peptides Interactions with Protein Nanopores
4. Electroosmotic Trap Against the Electrophoretic Force Near a Protein Nanopore Reveals Peptide Dynamics During Capture and Translocation
5. Protein Nanopore-Based Discrimination between Selected Neutral Amino Acids from Polypeptides
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