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(S)Pinning down protein interactions by NMR

Protein molecules are highly diverse communication platforms and their interaction repertoire stretches from atoms over small molecules such as sugars and lipids to macromolecules. An important route to understanding molecular communication is to quantitatively describe their interactions. These typ...

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Autores principales: Teilum, Kaare, Kunze, Micha Ben Achim, Erlendsson, Simon, Kragelund, Birthe B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5326574/
https://www.ncbi.nlm.nih.gov/pubmed/28019676
http://dx.doi.org/10.1002/pro.3105
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author Teilum, Kaare
Kunze, Micha Ben Achim
Erlendsson, Simon
Kragelund, Birthe B.
author_facet Teilum, Kaare
Kunze, Micha Ben Achim
Erlendsson, Simon
Kragelund, Birthe B.
author_sort Teilum, Kaare
collection PubMed
description Protein molecules are highly diverse communication platforms and their interaction repertoire stretches from atoms over small molecules such as sugars and lipids to macromolecules. An important route to understanding molecular communication is to quantitatively describe their interactions. These types of analyses determine the amounts and proportions of individual constituents that participate in a reaction as well as their rates of reactions and their thermodynamics. Although many different methods are available, there is currently no single method able to quantitatively capture and describe all types of protein reactions, which can span orders of magnitudes in affinities, reaction rates, and lifetimes of states. As the more versatile technique, solution NMR spectroscopy offers a remarkable catalogue of methods that can be successfully applied to the quantitative as well as qualitative descriptions of protein interactions. In this review we provide an easy‐access approach to NMR for the non‐NMR specialist and describe how and when solution state NMR spectroscopy is the method of choice for addressing protein ligand interaction. We describe very briefly the theoretical background and illustrate simple protein–ligand interactions as well as typical strategies for measuring binding constants using NMR spectroscopy. Finally, this review provides examples of caveats of the method as well as the options to improve the outcome of an NMR analysis of a protein interaction reaction.
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spelling pubmed-53265742017-03-01 (S)Pinning down protein interactions by NMR Teilum, Kaare Kunze, Micha Ben Achim Erlendsson, Simon Kragelund, Birthe B. Protein Sci Reviews Protein molecules are highly diverse communication platforms and their interaction repertoire stretches from atoms over small molecules such as sugars and lipids to macromolecules. An important route to understanding molecular communication is to quantitatively describe their interactions. These types of analyses determine the amounts and proportions of individual constituents that participate in a reaction as well as their rates of reactions and their thermodynamics. Although many different methods are available, there is currently no single method able to quantitatively capture and describe all types of protein reactions, which can span orders of magnitudes in affinities, reaction rates, and lifetimes of states. As the more versatile technique, solution NMR spectroscopy offers a remarkable catalogue of methods that can be successfully applied to the quantitative as well as qualitative descriptions of protein interactions. In this review we provide an easy‐access approach to NMR for the non‐NMR specialist and describe how and when solution state NMR spectroscopy is the method of choice for addressing protein ligand interaction. We describe very briefly the theoretical background and illustrate simple protein–ligand interactions as well as typical strategies for measuring binding constants using NMR spectroscopy. Finally, this review provides examples of caveats of the method as well as the options to improve the outcome of an NMR analysis of a protein interaction reaction. John Wiley and Sons Inc. 2017-02-14 2017-03 /pmc/articles/PMC5326574/ /pubmed/28019676 http://dx.doi.org/10.1002/pro.3105 Text en Published by Wiley‐Blackwell. © 2016 The Authors Protein Science published by Wiley Periodicals, Inc. on behalf of The Protein Society This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Reviews
Teilum, Kaare
Kunze, Micha Ben Achim
Erlendsson, Simon
Kragelund, Birthe B.
(S)Pinning down protein interactions by NMR
title (S)Pinning down protein interactions by NMR
title_full (S)Pinning down protein interactions by NMR
title_fullStr (S)Pinning down protein interactions by NMR
title_full_unstemmed (S)Pinning down protein interactions by NMR
title_short (S)Pinning down protein interactions by NMR
title_sort (s)pinning down protein interactions by nmr
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5326574/
https://www.ncbi.nlm.nih.gov/pubmed/28019676
http://dx.doi.org/10.1002/pro.3105
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