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Chaperonin Structure – The Large Multi-Subunit Protein Complex

The multi sub-unit protein structure representing the chaperonins group is analyzed with respect to its hydrophobicity distribution. The proteins of this group assist protein folding supported by ATP. The specific axial symmetry GroEL structure (two rings of seven units stacked back to back - 524 aa...

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Detalles Bibliográficos
Autores principales: Banach, Mateusz, Stąpor, Katarzyna, Roterman, Irena
Formato: Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2672005/
https://www.ncbi.nlm.nih.gov/pubmed/19399224
http://dx.doi.org/10.3390/ijms10030844
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author Banach, Mateusz
Stąpor, Katarzyna
Roterman, Irena
author_facet Banach, Mateusz
Stąpor, Katarzyna
Roterman, Irena
author_sort Banach, Mateusz
collection PubMed
description The multi sub-unit protein structure representing the chaperonins group is analyzed with respect to its hydrophobicity distribution. The proteins of this group assist protein folding supported by ATP. The specific axial symmetry GroEL structure (two rings of seven units stacked back to back - 524 aa each) and the GroES (single ring of seven units - 97 aa each) polypeptide chains are analyzed using the hydrophobicity distribution expressed as excess/deficiency all over the molecule to search for structure-to-function relationships. The empirically observed distribution of hydrophobic residues is confronted with the theoretical one representing the idealized hydrophobic core with hydrophilic residues exposure on the surface. The observed discrepancy between these two distributions seems to be aim-oriented, determining the structure-to-function relation. The hydrophobic force field structure generated by the chaperonin capsule is presented. Its possible influence on substrate folding is suggested.
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spelling pubmed-26720052009-04-27 Chaperonin Structure – The Large Multi-Subunit Protein Complex Banach, Mateusz Stąpor, Katarzyna Roterman, Irena Int J Mol Sci Article The multi sub-unit protein structure representing the chaperonins group is analyzed with respect to its hydrophobicity distribution. The proteins of this group assist protein folding supported by ATP. The specific axial symmetry GroEL structure (two rings of seven units stacked back to back - 524 aa each) and the GroES (single ring of seven units - 97 aa each) polypeptide chains are analyzed using the hydrophobicity distribution expressed as excess/deficiency all over the molecule to search for structure-to-function relationships. The empirically observed distribution of hydrophobic residues is confronted with the theoretical one representing the idealized hydrophobic core with hydrophilic residues exposure on the surface. The observed discrepancy between these two distributions seems to be aim-oriented, determining the structure-to-function relation. The hydrophobic force field structure generated by the chaperonin capsule is presented. Its possible influence on substrate folding is suggested. Molecular Diversity Preservation International (MDPI) 2009-03-02 /pmc/articles/PMC2672005/ /pubmed/19399224 http://dx.doi.org/10.3390/ijms10030844 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 Article
Banach, Mateusz
Stąpor, Katarzyna
Roterman, Irena
Chaperonin Structure – The Large Multi-Subunit Protein Complex
title Chaperonin Structure – The Large Multi-Subunit Protein Complex
title_full Chaperonin Structure – The Large Multi-Subunit Protein Complex
title_fullStr Chaperonin Structure – The Large Multi-Subunit Protein Complex
title_full_unstemmed Chaperonin Structure – The Large Multi-Subunit Protein Complex
title_short Chaperonin Structure – The Large Multi-Subunit Protein Complex
title_sort chaperonin structure – the large multi-subunit protein complex
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2672005/
https://www.ncbi.nlm.nih.gov/pubmed/19399224
http://dx.doi.org/10.3390/ijms10030844
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