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

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Globular and disordered-the non-identical twins in protein-protein interactions. / Teilum, Kaare; Olsen, Johan Gotthardt; Kragelund, Birthe Brandt.

I: Frontiers in Bioscience, Bind 2, 40, 2015.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Teilum, K, Olsen, JG & Kragelund, BB 2015, 'Globular and disordered-the non-identical twins in protein-protein interactions', Frontiers in Bioscience, bind 2, 40. https://doi.org/10.3389/fmolb.2015.00040

APA

Teilum, K., Olsen, J. G., & Kragelund, B. B. (2015). Globular and disordered-the non-identical twins in protein-protein interactions. Frontiers in Bioscience, 2, [40]. https://doi.org/10.3389/fmolb.2015.00040

Vancouver

Teilum K, Olsen JG, Kragelund BB. Globular and disordered-the non-identical twins in protein-protein interactions. Frontiers in Bioscience. 2015;2. 40. https://doi.org/10.3389/fmolb.2015.00040

Author

Teilum, Kaare ; Olsen, Johan Gotthardt ; Kragelund, Birthe Brandt. / Globular and disordered-the non-identical twins in protein-protein interactions. I: Frontiers in Bioscience. 2015 ; Bind 2.

Bibtex

@article{e33fe206db4d4f418875b7ef9c043cd1,
title = "Globular and disordered-the non-identical twins in protein-protein interactions",
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).",
author = "Kaare Teilum and Olsen, {Johan Gotthardt} and Kragelund, {Birthe Brandt}",
year = "2015",
doi = "10.3389/fmolb.2015.00040",
language = "English",
volume = "2",
journal = "Frontiers in Bioscience",
issn = "1093-9946",
publisher = "Frontiers in Bioscience",

}

RIS

TY - JOUR

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

Y1 - 2015

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).

U2 - 10.3389/fmolb.2015.00040

DO - 10.3389/fmolb.2015.00040

M3 - Journal article

C2 - 26217672

VL - 2

JO - Frontiers in Bioscience

JF - Frontiers in Bioscience

SN - 1093-9946

M1 - 40

ER -

ID: 141777669