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βB1-Crystallin: Thermodynamic Profiles of Molecular Interactions
BACKGROUND: β-Crystallins are structural proteins maintaining eye lens transparency and opacification. Previous work demonstrated that dimerization of both βA3 and βB2 crystallins (βA3 and βB2) involves endothermic enthalpy of association (∼8 kcal/mol) mediated by hydrophobic interactions. METHODOLO...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3253074/ https://www.ncbi.nlm.nih.gov/pubmed/22238594 http://dx.doi.org/10.1371/journal.pone.0029227 |
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author | Dolinska, Monika B. Wingfield, Paul T. Sergeev, Yuri V. |
author_facet | Dolinska, Monika B. Wingfield, Paul T. Sergeev, Yuri V. |
author_sort | Dolinska, Monika B. |
collection | PubMed |
description | BACKGROUND: β-Crystallins are structural proteins maintaining eye lens transparency and opacification. Previous work demonstrated that dimerization of both βA3 and βB2 crystallins (βA3 and βB2) involves endothermic enthalpy of association (∼8 kcal/mol) mediated by hydrophobic interactions. METHODOLOGY/PRINCIPAL FINDINGS: Thermodynamic profiles of the associations of dimeric βA3 and βB1 and tetrameric βB1/βA3 were measured using sedimentation equilibrium. The homo- and heteromolecular associations of βB1 crystallin are dominated by exothermic enthalpy (−13.3 and −24.5 kcal/mol, respectively). CONCLUSIONS/SIGNIFICANCE: Global thermodynamics of βB1 interactions suggest a role in the formation of stable protein complexes in the lens via specific van der Waals contacts, hydrogen bonds and salt bridges whereas those β-crystallins which associate by predominately hydrophobic forces participate in a weaker protein associations. |
format | Online Article Text |
id | pubmed-3253074 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-32530742012-01-11 βB1-Crystallin: Thermodynamic Profiles of Molecular Interactions Dolinska, Monika B. Wingfield, Paul T. Sergeev, Yuri V. PLoS One Research Article BACKGROUND: β-Crystallins are structural proteins maintaining eye lens transparency and opacification. Previous work demonstrated that dimerization of both βA3 and βB2 crystallins (βA3 and βB2) involves endothermic enthalpy of association (∼8 kcal/mol) mediated by hydrophobic interactions. METHODOLOGY/PRINCIPAL FINDINGS: Thermodynamic profiles of the associations of dimeric βA3 and βB1 and tetrameric βB1/βA3 were measured using sedimentation equilibrium. The homo- and heteromolecular associations of βB1 crystallin are dominated by exothermic enthalpy (−13.3 and −24.5 kcal/mol, respectively). CONCLUSIONS/SIGNIFICANCE: Global thermodynamics of βB1 interactions suggest a role in the formation of stable protein complexes in the lens via specific van der Waals contacts, hydrogen bonds and salt bridges whereas those β-crystallins which associate by predominately hydrophobic forces participate in a weaker protein associations. Public Library of Science 2012-01-06 /pmc/articles/PMC3253074/ /pubmed/22238594 http://dx.doi.org/10.1371/journal.pone.0029227 Text en This is an open-access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication. https://creativecommons.org/publicdomain/zero/1.0/ This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. |
spellingShingle | Research Article Dolinska, Monika B. Wingfield, Paul T. Sergeev, Yuri V. βB1-Crystallin: Thermodynamic Profiles of Molecular Interactions |
title | βB1-Crystallin: Thermodynamic Profiles of Molecular Interactions |
title_full | βB1-Crystallin: Thermodynamic Profiles of Molecular Interactions |
title_fullStr | βB1-Crystallin: Thermodynamic Profiles of Molecular Interactions |
title_full_unstemmed | βB1-Crystallin: Thermodynamic Profiles of Molecular Interactions |
title_short | βB1-Crystallin: Thermodynamic Profiles of Molecular Interactions |
title_sort | βb1-crystallin: thermodynamic profiles of molecular interactions |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3253074/ https://www.ncbi.nlm.nih.gov/pubmed/22238594 http://dx.doi.org/10.1371/journal.pone.0029227 |
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