Correlations within polyprotein forced unfolding dwell-times introduce sequential dependency.
AFM
Correlations
Force-spectroscopy
Non-exponential kinetics
Polyprotein
Single-molecule
Journal
Journal of structural biology
ISSN: 1095-8657
Titre abrégé: J Struct Biol
Pays: United States
ID NLM: 9011206
Informations de publication
Date de publication:
01 06 2020
01 06 2020
Historique:
received:
30
11
2019
revised:
15
02
2020
accepted:
11
03
2020
pubmed:
17
3
2020
medline:
20
7
2021
entrez:
17
3
2020
Statut:
ppublish
Résumé
Polyproteins, comprised from proteins arrayed in tandem, respond to mechanical loads through partial unfolding and extension. This response to tension that enables their physiological function is related to the ability to dynamically regulate their elasticity. The unique arrangement of their individual mechanical components (proteins and polymeric linkers), and the interactions between them eventually determines their performance. The sequential unfolding-times within a polyprotein are inherently assumed to be independent and identically distributed (iid), thus expected to follow an exponential distribution. Nevertheless, a large body of literature using single molecule force spectroscopy (SMFS) provides evidence that forced unfolding-times of N proteins within a polyprotein do not follow the exponential distribution. Here we use SMFS with Atomic Force Microscopy to measure the unfolding kinetics of Poly-(I91)
Identifiants
pubmed: 32173465
pii: S1047-8477(20)30061-7
doi: 10.1016/j.jsb.2020.107495
pii:
doi:
Substances chimiques
Polyproteins
0
Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
107495Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.