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Role of Water in Protein Folding and Activity

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Informatics".

Deadline for manuscript submissions: closed (30 November 2021) | Viewed by 3783

Special Issue Editors


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Guest Editor
Department of Bioinformatics and Telemedicine, Uniwersytet Jagielloński Collegium Medicum, 31-008 Kraków, Poland
Interests: bioinformatics-proteomics; protein structure prediction; amyloidosis; systems biology; construction of proteome; simulation in medicine

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Guest Editor
Gdańsk University of Technology, Gdansk, Poland

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Guest Editor
Wrocław University of Science and Technology, Wroclaw, Poland

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Guest Editor
Silesian University of Technology, Gliwice, Poland

Special Issue Information

Dear Colleagues,

The role of water in determining the biological activity of proteins is of primary importance. Life as we know it on our planet is designed to be active in the aquatic environment. This condition is so obvious that it does not get enough attention. Models of biomolecular systems including water mainly use representations of the set of individual water molecules and their interactions at the atomic level. The model of the water environment conditioning biological activity deserves much more attention. Therefore, this Special Issue is addressed to Authors studying the properties of the water environment to encourage them to present their results.

The phenomenon of the construction of spherical micelles formed by bipolar particles is an example of the effects of the presence of an external field. The formation of micelles is an expression of the influence of the water environment on the processes taking place in it.

The interaction of the water environment with the hydrophobic surface is of particular importance. High hydrophobicity, exposed locally on the surface of proteins, is important for the communication between molecules. The search for a mechanism accompanying this phenomenon is of critical importance for the recognition of processes described as specific, because the flow of communication through water determines the course of these and many other processes.

Dr. Irena Roterman-Konieczna
Dr. Jan Zielkiewicz
Dr. Andrzej Sokalski
Dr. Katarzyna Stapor
Guest Editors

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Keywords

  • amyloids
  • amyloid transformation
  • downhill folding
  • edge ß-strand
  • information entropy
  • external force field
  • hydrophobic core
  • hydrophobicity
  • negative feedback loop
  • protein folding
  • water environment
  • active participation of water in folding process

Published Papers (2 papers)

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26 pages, 9971 KiB  
Article
In Silico Modeling of the Influence of Environment on Amyloid Folding Using FOD-M Model
by Irena Roterman, Katarzyna Stapor, Piotr Fabian and Leszek Konieczny
Int. J. Mol. Sci. 2021, 22(19), 10587; https://doi.org/10.3390/ijms221910587 - 30 Sep 2021
Cited by 11 | Viewed by 1740
Abstract
The role of the environment in amyloid formation based on the fuzzy oil drop model (FOD) is discussed here. This model assumes that the hydrophobicity distribution within a globular protein is consistent with a 3D Gaussian (3DG) distribution. Such a distribution is interpreted [...] Read more.
The role of the environment in amyloid formation based on the fuzzy oil drop model (FOD) is discussed here. This model assumes that the hydrophobicity distribution within a globular protein is consistent with a 3D Gaussian (3DG) distribution. Such a distribution is interpreted as the idealized effect of the presence of a polar solvent—water. A chain with a sequence of amino acids (which are bipolar molecules) determined by evolution recreates a micelle-like structure with varying accuracy. The membrane, which is a specific environment with opposite characteristics to the polar aquatic environment, directs the hydrophobic residues towards the surface. The modification of the FOD model to the FOD-M form takes into account the specificity of the cell membrane. It consists in “inverting” the 3DG distribution (complementing the Gaussian distribution), which expresses the exposure of hydrophobic residues on the surface. It turns out that the influence of the environment for any protein (soluble or membrane-anchored) is the result of a consensus factor expressing the participation of the polar environment and the “inverted” environment. The ratio between the proportion of the aqueous and the “reversed” environment turns out to be a characteristic property of a given protein, including amyloid protein in particular. The structure of amyloid proteins has been characterized in the context of prion, intrinsically disordered, and other non-complexing proteins to cover a wider spectrum of molecules with the given characteristics based on the FOD-M model. Full article
(This article belongs to the Special Issue Role of Water in Protein Folding and Activity)
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24 pages, 6343 KiB  
Article
Model of Environmental Membrane Field for Transmembrane Proteins
by Irena Roterman, Katarzyna Stapor, Piotr Fabian, Leszek Konieczny and Mateusz Banach
Int. J. Mol. Sci. 2021, 22(7), 3619; https://doi.org/10.3390/ijms22073619 - 31 Mar 2021
Cited by 21 | Viewed by 1561
Abstract
The water environment determines the activity of biological processes. The role of such an environment interpreted in the form of an external field expressed by the 3D Gaussian distribution in the fuzzy oil drop model directs the folding process towards the generation of [...] Read more.
The water environment determines the activity of biological processes. The role of such an environment interpreted in the form of an external field expressed by the 3D Gaussian distribution in the fuzzy oil drop model directs the folding process towards the generation of a centrally located hydrophobic core with the simultaneous exposure of polar residues on the surface. In addition to proteins soluble in the water environment, there is a significant group of membrane proteins that act as receptors or channels, including ion channels in particular. The change of the polar (water) environment into a highly hydrophobic (membrane) environment is quite radical, resulting in a different hydrophobicity distribution within the membrane protein. Modification of the notation of the force field expressing the presence of the hydrophobic environment has been proposed in this work. A modified fuzzy oil drop model with its adaptation to membrane proteins was used to interpret the structure of membrane proteins–mechanosensitive channel. The modified model was also used to describe the so-called negative cases—i.e., for water-soluble proteins with a clear distribution consistent with the fuzzy oil drop model. Full article
(This article belongs to the Special Issue Role of Water in Protein Folding and Activity)
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