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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...

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Detalles Bibliográficos
Autores principales: Björklund, Emil, du Rietz, Anna, Lundström, Patrik
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons, Inc. 2021
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.
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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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