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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2017
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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. |
format | Online Article Text |
id | pubmed-5326574 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
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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