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The Contribution of Hydrophobic Interactions to Conformational Changes of Inward/Outward Transmembrane Transport Proteins

Proteins transporting ions or other molecules across the membrane, whose proper concentration is required to maintain homeostasis, perform very sophisticated biological functions. The symport and antiport active transport can be performed only by the structures specially prepared for this purpose. I...

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Detalles Bibliográficos
Autores principales: Roterman, Irena, Stapor, Katarzyna, Konieczny, Leszek
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9784565/
https://www.ncbi.nlm.nih.gov/pubmed/36557119
http://dx.doi.org/10.3390/membranes12121212
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author Roterman, Irena
Stapor, Katarzyna
Konieczny, Leszek
author_facet Roterman, Irena
Stapor, Katarzyna
Konieczny, Leszek
author_sort Roterman, Irena
collection PubMed
description Proteins transporting ions or other molecules across the membrane, whose proper concentration is required to maintain homeostasis, perform very sophisticated biological functions. The symport and antiport active transport can be performed only by the structures specially prepared for this purpose. In the present work, such structures in both In and Out conformations have been analyzed with respect to the hydrophobicity distribution using the FOD-M model. This allowed for identifying the role of individual protein chain fragments in the stabilization of the specific cell membrane environment as well as the contribution of hydrophobic interactions to the conformational changes between In/Out conformations.
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spelling pubmed-97845652022-12-24 The Contribution of Hydrophobic Interactions to Conformational Changes of Inward/Outward Transmembrane Transport Proteins Roterman, Irena Stapor, Katarzyna Konieczny, Leszek Membranes (Basel) Article Proteins transporting ions or other molecules across the membrane, whose proper concentration is required to maintain homeostasis, perform very sophisticated biological functions. The symport and antiport active transport can be performed only by the structures specially prepared for this purpose. In the present work, such structures in both In and Out conformations have been analyzed with respect to the hydrophobicity distribution using the FOD-M model. This allowed for identifying the role of individual protein chain fragments in the stabilization of the specific cell membrane environment as well as the contribution of hydrophobic interactions to the conformational changes between In/Out conformations. MDPI 2022-11-30 /pmc/articles/PMC9784565/ /pubmed/36557119 http://dx.doi.org/10.3390/membranes12121212 Text en © 2022 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
Konieczny, Leszek
The Contribution of Hydrophobic Interactions to Conformational Changes of Inward/Outward Transmembrane Transport Proteins
title The Contribution of Hydrophobic Interactions to Conformational Changes of Inward/Outward Transmembrane Transport Proteins
title_full The Contribution of Hydrophobic Interactions to Conformational Changes of Inward/Outward Transmembrane Transport Proteins
title_fullStr The Contribution of Hydrophobic Interactions to Conformational Changes of Inward/Outward Transmembrane Transport Proteins
title_full_unstemmed The Contribution of Hydrophobic Interactions to Conformational Changes of Inward/Outward Transmembrane Transport Proteins
title_short The Contribution of Hydrophobic Interactions to Conformational Changes of Inward/Outward Transmembrane Transport Proteins
title_sort contribution of hydrophobic interactions to conformational changes of inward/outward transmembrane transport proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9784565/
https://www.ncbi.nlm.nih.gov/pubmed/36557119
http://dx.doi.org/10.3390/membranes12121212
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