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Primary structure of proteins as a nanowire for metabolic electronic transport
It is considered that the major process in an organism is the synthesis of the adenosine triphosphate (ATP) molecules (its resumption from the adenosine diphosphate (ADP) molecules). These molecules are the basic (if not unique) energy resource of an organism. For the completion of process of the AT...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer US
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4385245/ https://www.ncbi.nlm.nih.gov/pubmed/25852414 http://dx.doi.org/10.1186/s11671-015-0763-0 |
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author | Suprun, Anatol D Shmeleva, Liudmyla V |
author_facet | Suprun, Anatol D Shmeleva, Liudmyla V |
author_sort | Suprun, Anatol D |
collection | PubMed |
description | It is considered that the major process in an organism is the synthesis of the adenosine triphosphate (ATP) molecules (its resumption from the adenosine diphosphate (ADP) molecules). These molecules are the basic (if not unique) energy resource of an organism. For the completion of process of the ATP synthesis in mitochondria, it is necessary to transfer to it a pair of electrons from places where electrons rise up as a result of oxidizing processes. Research of mechanisms of such transfer is important therefore, in particular, from the point of regulative influence on them in medical aims. Various proteins, the primary structure of which can provide the transport of electrons between donors and acceptors, saturate a volume and membranes of cages. A question about a possibility to examine this primary structure of proteins as a nanowire of a semiconductor nature is analyzed. The possibility of active transport of electrons through its conductivity band is analyzed also. In this paper, it was shown that a heterogeneous protein system is possible to be considered as a semiconductor with an average-nitrogen nuclear subsystem and with an average-oxygen electronic subsystem. Also, it was shown that in the potential energy of interaction between the electron and the nuclear subsystem indeed exists non-compensated contributions. These contributions are related to the radicals and provide the active transport of electrons along the primary structure of protein molecules. It was demonstrated also that external fields can have local regulative influence on the transport of electron in proteins by compensating the remaining field or strengthening it. Fulfilled analysis gives a possibility in zero approximation of the application of representation of numbers of filling to the protein molecule, considering it as the nanowire. |
format | Online Article Text |
id | pubmed-4385245 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Springer US |
record_format | MEDLINE/PubMed |
spelling | pubmed-43852452015-04-07 Primary structure of proteins as a nanowire for metabolic electronic transport Suprun, Anatol D Shmeleva, Liudmyla V Nanoscale Res Lett Nano Express It is considered that the major process in an organism is the synthesis of the adenosine triphosphate (ATP) molecules (its resumption from the adenosine diphosphate (ADP) molecules). These molecules are the basic (if not unique) energy resource of an organism. For the completion of process of the ATP synthesis in mitochondria, it is necessary to transfer to it a pair of electrons from places where electrons rise up as a result of oxidizing processes. Research of mechanisms of such transfer is important therefore, in particular, from the point of regulative influence on them in medical aims. Various proteins, the primary structure of which can provide the transport of electrons between donors and acceptors, saturate a volume and membranes of cages. A question about a possibility to examine this primary structure of proteins as a nanowire of a semiconductor nature is analyzed. The possibility of active transport of electrons through its conductivity band is analyzed also. In this paper, it was shown that a heterogeneous protein system is possible to be considered as a semiconductor with an average-nitrogen nuclear subsystem and with an average-oxygen electronic subsystem. Also, it was shown that in the potential energy of interaction between the electron and the nuclear subsystem indeed exists non-compensated contributions. These contributions are related to the radicals and provide the active transport of electrons along the primary structure of protein molecules. It was demonstrated also that external fields can have local regulative influence on the transport of electron in proteins by compensating the remaining field or strengthening it. Fulfilled analysis gives a possibility in zero approximation of the application of representation of numbers of filling to the protein molecule, considering it as the nanowire. Springer US 2015-03-12 /pmc/articles/PMC4385245/ /pubmed/25852414 http://dx.doi.org/10.1186/s11671-015-0763-0 Text en © Suprun and Shmeleva; licensee Springer. 2015 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. |
spellingShingle | Nano Express Suprun, Anatol D Shmeleva, Liudmyla V Primary structure of proteins as a nanowire for metabolic electronic transport |
title | Primary structure of proteins as a nanowire for metabolic electronic transport |
title_full | Primary structure of proteins as a nanowire for metabolic electronic transport |
title_fullStr | Primary structure of proteins as a nanowire for metabolic electronic transport |
title_full_unstemmed | Primary structure of proteins as a nanowire for metabolic electronic transport |
title_short | Primary structure of proteins as a nanowire for metabolic electronic transport |
title_sort | primary structure of proteins as a nanowire for metabolic electronic transport |
topic | Nano Express |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4385245/ https://www.ncbi.nlm.nih.gov/pubmed/25852414 http://dx.doi.org/10.1186/s11671-015-0763-0 |
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