Journal
MEMBRANES
Volume 12, Issue 1, Pages -Publisher
MDPI
DOI: 10.3390/membranes12010050
Keywords
membrane proteins; hydrophobicity; hydrophobic core; MscS; mechanosensitive channels; efflux in bacteria; MsbA
Categories
Funding
- Jagiellonian University Medical College [N41/DBS/000722]
- [857533]
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This study characterized the structures of water-soluble proteins and membrane proteins using the fuzzy oil drop model. The analysis aimed to verify the potential use of an external force field in simulating the protein-folding process while considering the diverse nature of the environment that ensures a biologically active structure.
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.
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