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Energy Transport along α-Helix Protein Chains: External Drives and Multifractal Analysis

Energy transport within biological systems is critical for biological functions in living cells and for technological applications in molecular motors. Biological systems have very complex dynamics supporting a large number of biochemical and biophysical processes. In the current work, we study the...

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Autores principales: Sefidkar, Narmin, Fathizadeh, Samira, Nemati, Fatemeh, Simserides, Constantinos
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9029186/
https://www.ncbi.nlm.nih.gov/pubmed/35454472
http://dx.doi.org/10.3390/ma15082779
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author Sefidkar, Narmin
Fathizadeh, Samira
Nemati, Fatemeh
Simserides, Constantinos
author_facet Sefidkar, Narmin
Fathizadeh, Samira
Nemati, Fatemeh
Simserides, Constantinos
author_sort Sefidkar, Narmin
collection PubMed
description Energy transport within biological systems is critical for biological functions in living cells and for technological applications in molecular motors. Biological systems have very complex dynamics supporting a large number of biochemical and biophysical processes. In the current work, we study the energy transport along protein chains. We examine the influence of different factors such as temperature, salt concentration, and external mechanical drive on the energy flux through protein chains. We obtain that energy fluctuations around the average value for short chains are greater than for longer chains. In addition, the external mechanical load is the most effective agent on bioenergy transport along the studied protein systems. Our results can help design a functional nano-scaled molecular motor based on energy transport along protein chains.
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spelling pubmed-90291862022-04-23 Energy Transport along α-Helix Protein Chains: External Drives and Multifractal Analysis Sefidkar, Narmin Fathizadeh, Samira Nemati, Fatemeh Simserides, Constantinos Materials (Basel) Article Energy transport within biological systems is critical for biological functions in living cells and for technological applications in molecular motors. Biological systems have very complex dynamics supporting a large number of biochemical and biophysical processes. In the current work, we study the energy transport along protein chains. We examine the influence of different factors such as temperature, salt concentration, and external mechanical drive on the energy flux through protein chains. We obtain that energy fluctuations around the average value for short chains are greater than for longer chains. In addition, the external mechanical load is the most effective agent on bioenergy transport along the studied protein systems. Our results can help design a functional nano-scaled molecular motor based on energy transport along protein chains. MDPI 2022-04-10 /pmc/articles/PMC9029186/ /pubmed/35454472 http://dx.doi.org/10.3390/ma15082779 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
Sefidkar, Narmin
Fathizadeh, Samira
Nemati, Fatemeh
Simserides, Constantinos
Energy Transport along α-Helix Protein Chains: External Drives and Multifractal Analysis
title Energy Transport along α-Helix Protein Chains: External Drives and Multifractal Analysis
title_full Energy Transport along α-Helix Protein Chains: External Drives and Multifractal Analysis
title_fullStr Energy Transport along α-Helix Protein Chains: External Drives and Multifractal Analysis
title_full_unstemmed Energy Transport along α-Helix Protein Chains: External Drives and Multifractal Analysis
title_short Energy Transport along α-Helix Protein Chains: External Drives and Multifractal Analysis
title_sort energy transport along α-helix protein chains: external drives and multifractal analysis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9029186/
https://www.ncbi.nlm.nih.gov/pubmed/35454472
http://dx.doi.org/10.3390/ma15082779
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