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Dependence of Protein Structure on Environment: FOD Model Applied to Membrane Proteins

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 an...

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Autores principales: Roterman, Irena, Stapor, Katarzyna, Gądek, Krzysztof, Gubała, Tomasz, Nowakowski, Piotr, Fabian, Piotr, Konieczny, Leszek
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8778870/
https://www.ncbi.nlm.nih.gov/pubmed/35054576
http://dx.doi.org/10.3390/membranes12010050
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author Roterman, Irena
Stapor, Katarzyna
Gądek, Krzysztof
Gubała, Tomasz
Nowakowski, Piotr
Fabian, Piotr
Konieczny, Leszek
author_facet Roterman, Irena
Stapor, Katarzyna
Gądek, Krzysztof
Gubała, Tomasz
Nowakowski, Piotr
Fabian, Piotr
Konieczny, Leszek
author_sort Roterman, Irena
collection PubMed
description 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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spelling pubmed-87788702022-01-22 Dependence of Protein Structure on Environment: FOD Model Applied to Membrane Proteins Roterman, Irena Stapor, Katarzyna Gądek, Krzysztof Gubała, Tomasz Nowakowski, Piotr Fabian, Piotr Konieczny, Leszek Membranes (Basel) Article 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. MDPI 2021-12-30 /pmc/articles/PMC8778870/ /pubmed/35054576 http://dx.doi.org/10.3390/membranes12010050 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Roterman, Irena
Stapor, Katarzyna
Gądek, Krzysztof
Gubała, Tomasz
Nowakowski, Piotr
Fabian, Piotr
Konieczny, Leszek
Dependence of Protein Structure on Environment: FOD Model Applied to Membrane Proteins
title Dependence of Protein Structure on Environment: FOD Model Applied to Membrane Proteins
title_full Dependence of Protein Structure on Environment: FOD Model Applied to Membrane Proteins
title_fullStr Dependence of Protein Structure on Environment: FOD Model Applied to Membrane Proteins
title_full_unstemmed Dependence of Protein Structure on Environment: FOD Model Applied to Membrane Proteins
title_short Dependence of Protein Structure on Environment: FOD Model Applied to Membrane Proteins
title_sort dependence of protein structure on environment: fod model applied to membrane proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8778870/
https://www.ncbi.nlm.nih.gov/pubmed/35054576
http://dx.doi.org/10.3390/membranes12010050
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