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Mechanism of Suppression of Protein Aggregation by α-Crystallin
This review summarizes experimental data illuminating the mechanism of suppression of heat-induced protein aggregation by α-crystallin, one of the small heat shock proteins. The dynamic light scattering data show that the initial stage of thermal aggregation of proteins is the formation of the initi...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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Molecular Diversity Preservation International (MDPI)
2009
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2672032/ https://www.ncbi.nlm.nih.gov/pubmed/19399251 http://dx.doi.org/10.3390/ijms10031314 |
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author | Markossian, Kira A. Yudin, Igor K. Kurganov, Boris I. |
author_facet | Markossian, Kira A. Yudin, Igor K. Kurganov, Boris I. |
author_sort | Markossian, Kira A. |
collection | PubMed |
description | This review summarizes experimental data illuminating the mechanism of suppression of heat-induced protein aggregation by α-crystallin, one of the small heat shock proteins. The dynamic light scattering data show that the initial stage of thermal aggregation of proteins is the formation of the initial aggregates involving hundreds of molecules of the denatured protein. Further sticking of the starting aggregates proceeds in a regime of diffusion-limited cluster-cluster aggregation. The protective effect of α-crystallin is due to transition of the aggregation process to the regime of reaction-limited cluster-cluster aggregation, wherein the sticking probability for the colliding particles becomes lower than unity. |
format | Text |
id | pubmed-2672032 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
spelling | pubmed-26720322009-04-27 Mechanism of Suppression of Protein Aggregation by α-Crystallin Markossian, Kira A. Yudin, Igor K. Kurganov, Boris I. Int J Mol Sci Review This review summarizes experimental data illuminating the mechanism of suppression of heat-induced protein aggregation by α-crystallin, one of the small heat shock proteins. The dynamic light scattering data show that the initial stage of thermal aggregation of proteins is the formation of the initial aggregates involving hundreds of molecules of the denatured protein. Further sticking of the starting aggregates proceeds in a regime of diffusion-limited cluster-cluster aggregation. The protective effect of α-crystallin is due to transition of the aggregation process to the regime of reaction-limited cluster-cluster aggregation, wherein the sticking probability for the colliding particles becomes lower than unity. Molecular Diversity Preservation International (MDPI) 2009-03-19 /pmc/articles/PMC2672032/ /pubmed/19399251 http://dx.doi.org/10.3390/ijms10031314 Text en © 2009 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review Markossian, Kira A. Yudin, Igor K. Kurganov, Boris I. Mechanism of Suppression of Protein Aggregation by α-Crystallin |
title | Mechanism of Suppression of Protein Aggregation by α-Crystallin |
title_full | Mechanism of Suppression of Protein Aggregation by α-Crystallin |
title_fullStr | Mechanism of Suppression of Protein Aggregation by α-Crystallin |
title_full_unstemmed | Mechanism of Suppression of Protein Aggregation by α-Crystallin |
title_short | Mechanism of Suppression of Protein Aggregation by α-Crystallin |
title_sort | mechanism of suppression of protein aggregation by α-crystallin |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2672032/ https://www.ncbi.nlm.nih.gov/pubmed/19399251 http://dx.doi.org/10.3390/ijms10031314 |
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