Globular and disordered – the non-identical twins in protein-protein interactions

In biology proteins from different structural classes interact across and within classes in ways that are optimized to achieve balanced functional outputs. The interactions between intrinsically disordered proteins (IDPs) and other proteins rely on changes in flexibility and this is seen as a strong...

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Main Authors: Kaare eTeilum, Johan G. Olsen, Birthe B. eKragelund
Format: Article
Language:English
Published: Frontiers Media S.A. 2015-07-01
Series:Frontiers in Molecular Biosciences
Subjects:
Online Access:http://journal.frontiersin.org/Journal/10.3389/fmolb.2015.00040/full
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author Kaare eTeilum
Johan G. Olsen
Birthe B. eKragelund
author_facet Kaare eTeilum
Johan G. Olsen
Birthe B. eKragelund
author_sort Kaare eTeilum
collection DOAJ
description In biology proteins from different structural classes interact across and within classes in ways that are optimized to achieve balanced functional outputs. The interactions between intrinsically disordered proteins (IDPs) and other proteins rely on changes in flexibility and this is seen as a strong determinant for their function. This has fostered the notion that IDP’s bind with low affinity but high specificity. Here we have analyzed available detailed thermodynamic data for protein-protein interactions to put to the test if the thermodynamic profiles of IDP interactions differ from those of other protein-protein interactions. We find that ordered proteins and the disordered ones act as non identical twins operating by similar principles but where the disordered proteins complexes are on average less stable by 2.5 kcal mol-1.
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spelling doaj.art-3745adc6e0a84d569a1783318d4f04082022-12-22T01:55:55ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2015-07-01210.3389/fmolb.2015.00040150061Globular and disordered – the non-identical twins in protein-protein interactionsKaare eTeilum0Johan G. Olsen1Birthe B. eKragelund2University of CopenhagenUniversity of CopenhagenUniversity of CopenhagenIn biology proteins from different structural classes interact across and within classes in ways that are optimized to achieve balanced functional outputs. The interactions between intrinsically disordered proteins (IDPs) and other proteins rely on changes in flexibility and this is seen as a strong determinant for their function. This has fostered the notion that IDP’s bind with low affinity but high specificity. Here we have analyzed available detailed thermodynamic data for protein-protein interactions to put to the test if the thermodynamic profiles of IDP interactions differ from those of other protein-protein interactions. We find that ordered proteins and the disordered ones act as non identical twins operating by similar principles but where the disordered proteins complexes are on average less stable by 2.5 kcal mol-1.http://journal.frontiersin.org/Journal/10.3389/fmolb.2015.00040/fullstabilityentropyIDPenthalpyITCIntrinsically disordered
spellingShingle Kaare eTeilum
Johan G. Olsen
Birthe B. eKragelund
Globular and disordered – the non-identical twins in protein-protein interactions
Frontiers in Molecular Biosciences
stability
entropy
IDP
enthalpy
ITC
Intrinsically disordered
title Globular and disordered – the non-identical twins in protein-protein interactions
title_full Globular and disordered – the non-identical twins in protein-protein interactions
title_fullStr Globular and disordered – the non-identical twins in protein-protein interactions
title_full_unstemmed Globular and disordered – the non-identical twins in protein-protein interactions
title_short Globular and disordered – the non-identical twins in protein-protein interactions
title_sort globular and disordered the non identical twins in protein protein interactions
topic stability
entropy
IDP
enthalpy
ITC
Intrinsically disordered
url http://journal.frontiersin.org/Journal/10.3389/fmolb.2015.00040/full
work_keys_str_mv AT kaareeteilum globularanddisorderedthenonidenticaltwinsinproteinproteininteractions
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AT birthebekragelund globularanddisorderedthenonidenticaltwinsinproteinproteininteractions