Dependence of Protein Structure on Environment: FOD Model Applied to Membrane Proteins.
MsbA
MscS
efflux in bacteria
hydrophobic core
hydrophobicity
mechanosensitive channels
membrane proteins
Journal
Membranes
ISSN: 2077-0375
Titre abrégé: Membranes (Basel)
Pays: Switzerland
ID NLM: 101577807
Informations de publication
Date de publication:
30 Dec 2021
30 Dec 2021
Historique:
received:
16
11
2021
revised:
13
12
2021
accepted:
28
12
2021
entrez:
21
1
2022
pubmed:
22
1
2022
medline:
22
1
2022
Statut:
epublish
Résumé
The natural environment of proteins is the polar aquatic environment and the hydrophobic (amphipathic) environment of the membrane. The fuzzy oil drop model (FOD) used to characterize water-soluble proteins, as well as its modified version FOD-M, enables a mathematical description of the presence and influence of diverse environments on protein structure. The present work characterized the structures of membrane proteins, including those that act as channels, and a water-soluble protein for contrast. The purpose of the analysis was to verify the possibility that an external force field can be used in the simulation of the protein-folding process, taking into account the diverse nature of the environment that guarantees a structure showing biological activity.
Identifiants
pubmed: 35054576
pii: membranes12010050
doi: 10.3390/membranes12010050
pmc: PMC8778870
pii:
doi:
Types de publication
Journal Article
Langues
eng
Subventions
Organisme : Jagiellonian University
ID : N41/DBS/000722
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