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Energetic Calculations to Decipher pH-Dependent Oligomerization and Domain Swapping of Proteins

Domain swapping mechanism is a specialised mode of oligomerization of proteins in which part of a protein is exchanged in a non-covalent manner between constituent subunits. This mechanism is highly affected by several physiological conditions. Here, we present a detailed analysis ofthe effect of pH...

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Detalles Bibliográficos
Autores principales: Shingate, Prashant, Warwicker, Jim, Sowdhamini, Ramanathan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4456399/
https://www.ncbi.nlm.nih.gov/pubmed/26043007
http://dx.doi.org/10.1371/journal.pone.0127716
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author Shingate, Prashant
Warwicker, Jim
Sowdhamini, Ramanathan
author_facet Shingate, Prashant
Warwicker, Jim
Sowdhamini, Ramanathan
author_sort Shingate, Prashant
collection PubMed
description Domain swapping mechanism is a specialised mode of oligomerization of proteins in which part of a protein is exchanged in a non-covalent manner between constituent subunits. This mechanism is highly affected by several physiological conditions. Here, we present a detailed analysis ofthe effect of pH on different regions of the domain swapped oligomer by considering examples which are known to be sensitive to pH in transiting from monomeric to domain-swapped dimeric form. The energetic calculations were performed using a specialized method which considers changes in pH and subsequent changes in the interactions between subunits. This analysis provides definitive hints about the pH-dependence switch from monomer to domain-swapped oligomer and the steps that may be involved in the swapping mechanism.
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spelling pubmed-44563992015-06-09 Energetic Calculations to Decipher pH-Dependent Oligomerization and Domain Swapping of Proteins Shingate, Prashant Warwicker, Jim Sowdhamini, Ramanathan PLoS One Research Article Domain swapping mechanism is a specialised mode of oligomerization of proteins in which part of a protein is exchanged in a non-covalent manner between constituent subunits. This mechanism is highly affected by several physiological conditions. Here, we present a detailed analysis ofthe effect of pH on different regions of the domain swapped oligomer by considering examples which are known to be sensitive to pH in transiting from monomeric to domain-swapped dimeric form. The energetic calculations were performed using a specialized method which considers changes in pH and subsequent changes in the interactions between subunits. This analysis provides definitive hints about the pH-dependence switch from monomer to domain-swapped oligomer and the steps that may be involved in the swapping mechanism. Public Library of Science 2015-06-04 /pmc/articles/PMC4456399/ /pubmed/26043007 http://dx.doi.org/10.1371/journal.pone.0127716 Text en © 2015 Shingate 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
Shingate, Prashant
Warwicker, Jim
Sowdhamini, Ramanathan
Energetic Calculations to Decipher pH-Dependent Oligomerization and Domain Swapping of Proteins
title Energetic Calculations to Decipher pH-Dependent Oligomerization and Domain Swapping of Proteins
title_full Energetic Calculations to Decipher pH-Dependent Oligomerization and Domain Swapping of Proteins
title_fullStr Energetic Calculations to Decipher pH-Dependent Oligomerization and Domain Swapping of Proteins
title_full_unstemmed Energetic Calculations to Decipher pH-Dependent Oligomerization and Domain Swapping of Proteins
title_short Energetic Calculations to Decipher pH-Dependent Oligomerization and Domain Swapping of Proteins
title_sort energetic calculations to decipher ph-dependent oligomerization and domain swapping of proteins
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4456399/
https://www.ncbi.nlm.nih.gov/pubmed/26043007
http://dx.doi.org/10.1371/journal.pone.0127716
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