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Analysis of protein–ligand interactions from titrations and nuclear magnetic resonance relaxation dispersions
We present PLIS, a publicly available, open‐source software for the determination of protein–ligand dissociation constants that can be used to characterize biological processes or to shed light on biophysical aspects of interactions. PLIS can analyze data from titration experiments monitored by for...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley & Sons, Inc.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8740844/ https://www.ncbi.nlm.nih.gov/pubmed/34791737 http://dx.doi.org/10.1002/pro.4240 |
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author | Björklund, Emil du Rietz, Anna Lundström, Patrik |
author_facet | Björklund, Emil du Rietz, Anna Lundström, Patrik |
author_sort | Björklund, Emil |
collection | PubMed |
description | We present PLIS, a publicly available, open‐source software for the determination of protein–ligand dissociation constants that can be used to characterize biological processes or to shed light on biophysical aspects of interactions. PLIS can analyze data from titration experiments monitored by for instance fluorescence spectroscopy or from nuclear magnetic resonance relaxation dispersion experiments. In addition to analysis of experimental data, PLIS includes functionality for generation of synthetic data, useful for understanding how different parameters effect the data in order to better analyze experiments. |
format | Online Article Text |
id | pubmed-8740844 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley & Sons, Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-87408442022-01-12 Analysis of protein–ligand interactions from titrations and nuclear magnetic resonance relaxation dispersions Björklund, Emil du Rietz, Anna Lundström, Patrik Protein Sci Tools for Protein Science We present PLIS, a publicly available, open‐source software for the determination of protein–ligand dissociation constants that can be used to characterize biological processes or to shed light on biophysical aspects of interactions. PLIS can analyze data from titration experiments monitored by for instance fluorescence spectroscopy or from nuclear magnetic resonance relaxation dispersion experiments. In addition to analysis of experimental data, PLIS includes functionality for generation of synthetic data, useful for understanding how different parameters effect the data in order to better analyze experiments. John Wiley & Sons, Inc. 2021-11-30 2022-01 /pmc/articles/PMC8740844/ /pubmed/34791737 http://dx.doi.org/10.1002/pro.4240 Text en © 2021 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society. https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. |
spellingShingle | Tools for Protein Science Björklund, Emil du Rietz, Anna Lundström, Patrik Analysis of protein–ligand interactions from titrations and nuclear magnetic resonance relaxation dispersions |
title | Analysis of protein–ligand interactions from titrations and nuclear magnetic resonance relaxation dispersions |
title_full | Analysis of protein–ligand interactions from titrations and nuclear magnetic resonance relaxation dispersions |
title_fullStr | Analysis of protein–ligand interactions from titrations and nuclear magnetic resonance relaxation dispersions |
title_full_unstemmed | Analysis of protein–ligand interactions from titrations and nuclear magnetic resonance relaxation dispersions |
title_short | Analysis of protein–ligand interactions from titrations and nuclear magnetic resonance relaxation dispersions |
title_sort | analysis of protein–ligand interactions from titrations and nuclear magnetic resonance relaxation dispersions |
topic | Tools for Protein Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8740844/ https://www.ncbi.nlm.nih.gov/pubmed/34791737 http://dx.doi.org/10.1002/pro.4240 |
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