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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Format: | Article |
Language: | English |
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Frontiers Media S.A.
2015-07-01
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Series: | Frontiers in Molecular Biosciences |
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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. |
first_indexed | 2024-12-10T08:38:00Z |
format | Article |
id | doaj.art-3745adc6e0a84d569a1783318d4f0408 |
institution | Directory Open Access Journal |
issn | 2296-889X |
language | English |
last_indexed | 2024-12-10T08:38:00Z |
publishDate | 2015-07-01 |
publisher | Frontiers Media S.A. |
record_format | Article |
series | Frontiers in Molecular Biosciences |
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 AT johangolsen globularanddisorderedthenonidenticaltwinsinproteinproteininteractions AT birthebekragelund globularanddisorderedthenonidenticaltwinsinproteinproteininteractions |