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

Kaare Teilum; Johan Gotthardt Olsen; Birthe Brandt Kragelund

doi:10.3389/fmolb.2015.00040

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

Kaare Teilum, Johan Gotthardt Olsen, Birthe Brandt Kragelund

Biomolecular Sciences

18 Citationer (Scopus)

96 Downloads (Pure)

Abstract

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).

Originalsprog	Engelsk
Artikelnummer	40
Tidsskrift	Frontiers in Bioscience
Vol/bind	2
Antal sider	6
ISSN	1093-9946
DOI	https://doi.org/10.3389/fmolb.2015.00040
Status	Udgivet - 9 jul. 2015

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10.3389/fmolb.2015.00040

Globular and disordered-the non-identical twins in protein-protein interactionsForlagets udgivne version, 1,83 MB

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abstract = "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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T1 - Globular and disordered-the non-identical twins in protein-protein interactions

AU - Teilum, Kaare

AU - Olsen, Johan Gotthardt

AU - Kragelund, Birthe Brandt

PY - 2015/7/9

Y1 - 2015/7/9

N2 - 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).

AB - 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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DO - 10.3389/fmolb.2015.00040

M3 - Journal article

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JO - Frontiers in Bioscience

JF - Frontiers in Bioscience

M1 - 40

ER -

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

Abstract

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