Contrasting effect of ficoll on apo and holo forms of bacterial chemotaxis protein Y: Selective destabilization of the conformationally altered holo form.
Chemotaxis Y
Ficoll-70
Thermal stability
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
31 Mar 2023
31 Mar 2023
Historique:
received:
03
11
2022
revised:
13
01
2023
accepted:
28
01
2023
pubmed:
4
2
2023
medline:
9
3
2023
entrez:
3
2
2023
Statut:
ppublish
Résumé
Chemotaxis Y (CheY), upon metal binding, displays a drastic alteration in its structure and stability. This premise prompted us to study the effect of crowding on the two conformationally distinct states of the same test protein. A comparative analysis on the structure and thermal stability in the presence and absence of the macromolecular crowder, ficoll, and its monomeric unit, sucrose, revealed a contrasting effect of ficoll on the apo and holo forms. In the presence of ficoll while the thermal stability (T
Identifiants
pubmed: 36736516
pii: S0141-8130(23)00398-7
doi: 10.1016/j.ijbiomac.2023.123505
pii:
doi:
Substances chimiques
Ficoll
25702-74-3
Bacterial Proteins
0
Macromolecular Substances
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
123505Informations de copyright
Copyright © 2023 Elsevier B.V. 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.