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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Main Authors: Prashant Shingate, Jim Warwicker, Ramanathan Sowdhamini
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2015-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4456399?pdf=render
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author Prashant Shingate
Jim Warwicker
Ramanathan Sowdhamini
author_facet Prashant Shingate
Jim Warwicker
Ramanathan Sowdhamini
author_sort Prashant Shingate
collection DOAJ
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 doaj.art-6bf2e533cb9447e192325baf8b675a0b2022-12-22T03:58:29ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01106e012771610.1371/journal.pone.0127716Energetic Calculations to Decipher pH-Dependent Oligomerization and Domain Swapping of Proteins.Prashant ShingateJim WarwickerRamanathan SowdhaminiDomain 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.http://europepmc.org/articles/PMC4456399?pdf=render
spellingShingle Prashant Shingate
Jim Warwicker
Ramanathan Sowdhamini
Energetic Calculations to Decipher pH-Dependent Oligomerization and Domain Swapping of Proteins.
PLoS ONE
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
url http://europepmc.org/articles/PMC4456399?pdf=render
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