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Dynamic protein ligand interactions – insights from MS
Proteins undergo dynamic interactions with carbohydrates, lipids and nucleotides to form catalytic cores, fine‐tuned for different cellular actions. The study of dynamic interactions between proteins and their cognate ligands is therefore fundamental to the understanding of biological systems. Durin...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4154455/ https://www.ncbi.nlm.nih.gov/pubmed/24393119 http://dx.doi.org/10.1111/febs.12707 |
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author | Schmidt, Carla Robinson, Carol V. |
author_facet | Schmidt, Carla Robinson, Carol V. |
author_sort | Schmidt, Carla |
collection | PubMed |
description | Proteins undergo dynamic interactions with carbohydrates, lipids and nucleotides to form catalytic cores, fine‐tuned for different cellular actions. The study of dynamic interactions between proteins and their cognate ligands is therefore fundamental to the understanding of biological systems. During the last two decades MS, and its associated techniques, has become accepted as a method for the study of protein–ligand interactions, not only for covalent complexes, where the use of MS is well established, but also, and significantly for protein–ligand interactions, for noncovalent assemblies. In this review, we employ a broad definition of a ligand to encompass protein subunits, drug molecules, oligonucleotides, carbohydrates, and lipids. Under the appropriate conditions, MS can reveal the composition, heterogeneity and dynamics of these protein–ligand interactions, and in some cases their structural arrangements and binding affinities. Herein, we highlight MS approaches for studying protein–ligand complexes, including those containing integral membrane subunits, and showcase examples from recent literature. Specifically, we tabulate the myriad of methodologies, including hydrogen exchange, proteomics, hydroxyl radical footprinting, intact complexes, and crosslinking, which, when combined with MS, provide insights into conformational changes and subtle modifications in response to ligand‐binding interactions. |
format | Online Article Text |
id | pubmed-4154455 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies |
record_format | MEDLINE/PubMed |
spelling | pubmed-41544552014-09-22 Dynamic protein ligand interactions – insights from MS Schmidt, Carla Robinson, Carol V. FEBS J Minireviews Proteins undergo dynamic interactions with carbohydrates, lipids and nucleotides to form catalytic cores, fine‐tuned for different cellular actions. The study of dynamic interactions between proteins and their cognate ligands is therefore fundamental to the understanding of biological systems. During the last two decades MS, and its associated techniques, has become accepted as a method for the study of protein–ligand interactions, not only for covalent complexes, where the use of MS is well established, but also, and significantly for protein–ligand interactions, for noncovalent assemblies. In this review, we employ a broad definition of a ligand to encompass protein subunits, drug molecules, oligonucleotides, carbohydrates, and lipids. Under the appropriate conditions, MS can reveal the composition, heterogeneity and dynamics of these protein–ligand interactions, and in some cases their structural arrangements and binding affinities. Herein, we highlight MS approaches for studying protein–ligand complexes, including those containing integral membrane subunits, and showcase examples from recent literature. Specifically, we tabulate the myriad of methodologies, including hydrogen exchange, proteomics, hydroxyl radical footprinting, intact complexes, and crosslinking, which, when combined with MS, provide insights into conformational changes and subtle modifications in response to ligand‐binding interactions. Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies 2014-01-21 2014-04 /pmc/articles/PMC4154455/ /pubmed/24393119 http://dx.doi.org/10.1111/febs.12707 Text en © 2014 The Authors. FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/3.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Minireviews Schmidt, Carla Robinson, Carol V. Dynamic protein ligand interactions – insights from MS |
title | Dynamic protein ligand interactions – insights from MS |
title_full | Dynamic protein ligand interactions – insights from MS |
title_fullStr | Dynamic protein ligand interactions – insights from MS |
title_full_unstemmed | Dynamic protein ligand interactions – insights from MS |
title_short | Dynamic protein ligand interactions – insights from MS |
title_sort | dynamic protein ligand interactions – insights from ms |
topic | Minireviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4154455/ https://www.ncbi.nlm.nih.gov/pubmed/24393119 http://dx.doi.org/10.1111/febs.12707 |
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