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Differences in the Pathways of Proteins Unfolding Induced by Urea and Guanidine Hydrochloride: Molten Globule State and Aggregates
It was shown that at low concentrations guanidine hydrochloride (GdnHCl) can cause aggregation of proteins in partially folded state and that fluorescent dye 1-anilinonaphthalene-8-sulfonic acid (ANS) binds with these aggregates rather than with hydrophobic clusters on the surface of protein in molt...
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Formato: | Texto |
Lenguaje: | English |
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Public Library of Science
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2994796/ https://www.ncbi.nlm.nih.gov/pubmed/21152408 http://dx.doi.org/10.1371/journal.pone.0015035 |
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author | Povarova, Olga I. Kuznetsova, Irina M. Turoverov, Konstantin K. |
author_facet | Povarova, Olga I. Kuznetsova, Irina M. Turoverov, Konstantin K. |
author_sort | Povarova, Olga I. |
collection | PubMed |
description | It was shown that at low concentrations guanidine hydrochloride (GdnHCl) can cause aggregation of proteins in partially folded state and that fluorescent dye 1-anilinonaphthalene-8-sulfonic acid (ANS) binds with these aggregates rather than with hydrophobic clusters on the surface of protein in molten globule state. That is why the increase in ANS fluorescence intensity is often recorded in the pathway of protein denaturation by GdnHCl, but not by urea. So what was previously believed to be the molten globule state in the pathway of protein denaturation by GdnHCl, in reality, for some proteins represents the aggregates of partially folded molecules. |
format | Text |
id | pubmed-2994796 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-29947962010-12-08 Differences in the Pathways of Proteins Unfolding Induced by Urea and Guanidine Hydrochloride: Molten Globule State and Aggregates Povarova, Olga I. Kuznetsova, Irina M. Turoverov, Konstantin K. PLoS One Research Article It was shown that at low concentrations guanidine hydrochloride (GdnHCl) can cause aggregation of proteins in partially folded state and that fluorescent dye 1-anilinonaphthalene-8-sulfonic acid (ANS) binds with these aggregates rather than with hydrophobic clusters on the surface of protein in molten globule state. That is why the increase in ANS fluorescence intensity is often recorded in the pathway of protein denaturation by GdnHCl, but not by urea. So what was previously believed to be the molten globule state in the pathway of protein denaturation by GdnHCl, in reality, for some proteins represents the aggregates of partially folded molecules. Public Library of Science 2010-11-30 /pmc/articles/PMC2994796/ /pubmed/21152408 http://dx.doi.org/10.1371/journal.pone.0015035 Text en Povarova et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Povarova, Olga I. Kuznetsova, Irina M. Turoverov, Konstantin K. Differences in the Pathways of Proteins Unfolding Induced by Urea and Guanidine Hydrochloride: Molten Globule State and Aggregates |
title | Differences in the Pathways of Proteins Unfolding Induced by Urea and Guanidine Hydrochloride: Molten Globule State and Aggregates |
title_full | Differences in the Pathways of Proteins Unfolding Induced by Urea and Guanidine Hydrochloride: Molten Globule State and Aggregates |
title_fullStr | Differences in the Pathways of Proteins Unfolding Induced by Urea and Guanidine Hydrochloride: Molten Globule State and Aggregates |
title_full_unstemmed | Differences in the Pathways of Proteins Unfolding Induced by Urea and Guanidine Hydrochloride: Molten Globule State and Aggregates |
title_short | Differences in the Pathways of Proteins Unfolding Induced by Urea and Guanidine Hydrochloride: Molten Globule State and Aggregates |
title_sort | differences in the pathways of proteins unfolding induced by urea and guanidine hydrochloride: molten globule state and aggregates |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2994796/ https://www.ncbi.nlm.nih.gov/pubmed/21152408 http://dx.doi.org/10.1371/journal.pone.0015035 |
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