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Bayesian Data Integration Questions Classic Study on Protease Self-Digest Kinetics
[Image: see text] We combine Bayesian data integration with kinetic modeling to rigorously identify reaction mechanisms. This approach forces models to be consistent not only with kinetic measurements but with all available information. We revisit a classic study on trypsin self-digest acceleration...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2020
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7331054/ https://www.ncbi.nlm.nih.gov/pubmed/32637789 http://dx.doi.org/10.1021/acsomega.0c01109 |
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author | Tötsch, Niklas Hoffmann, Daniel |
author_facet | Tötsch, Niklas Hoffmann, Daniel |
author_sort | Tötsch, Niklas |
collection | PubMed |
description | [Image: see text] We combine Bayesian data integration with kinetic modeling to rigorously identify reaction mechanisms. This approach forces models to be consistent not only with kinetic measurements but with all available information. We revisit a classic study on trypsin self-digest acceleration by colloidal silica. Bayesian data integration reveals that the mechanism suggested in that study is inconsistent with its presented data. We propose an improved hypothesis. However, the detailed mechanism of the surface reaction cannot be inferred from the available data. |
format | Online Article Text |
id | pubmed-7331054 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-73310542020-07-06 Bayesian Data Integration Questions Classic Study on Protease Self-Digest Kinetics Tötsch, Niklas Hoffmann, Daniel ACS Omega [Image: see text] We combine Bayesian data integration with kinetic modeling to rigorously identify reaction mechanisms. This approach forces models to be consistent not only with kinetic measurements but with all available information. We revisit a classic study on trypsin self-digest acceleration by colloidal silica. Bayesian data integration reveals that the mechanism suggested in that study is inconsistent with its presented data. We propose an improved hypothesis. However, the detailed mechanism of the surface reaction cannot be inferred from the available data. American Chemical Society 2020-06-19 /pmc/articles/PMC7331054/ /pubmed/32637789 http://dx.doi.org/10.1021/acsomega.0c01109 Text en Copyright © 2020 American Chemical Society This is an open access article published under a Creative Commons Attribution (CC-BY) License (http://pubs.acs.org/page/policy/authorchoice_ccby_termsofuse.html) , which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited. |
spellingShingle | Tötsch, Niklas Hoffmann, Daniel Bayesian Data Integration Questions Classic Study on Protease Self-Digest Kinetics |
title | Bayesian Data Integration Questions Classic Study
on Protease Self-Digest Kinetics |
title_full | Bayesian Data Integration Questions Classic Study
on Protease Self-Digest Kinetics |
title_fullStr | Bayesian Data Integration Questions Classic Study
on Protease Self-Digest Kinetics |
title_full_unstemmed | Bayesian Data Integration Questions Classic Study
on Protease Self-Digest Kinetics |
title_short | Bayesian Data Integration Questions Classic Study
on Protease Self-Digest Kinetics |
title_sort | bayesian data integration questions classic study
on protease self-digest kinetics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7331054/ https://www.ncbi.nlm.nih.gov/pubmed/32637789 http://dx.doi.org/10.1021/acsomega.0c01109 |
work_keys_str_mv | AT totschniklas bayesiandataintegrationquestionsclassicstudyonproteaseselfdigestkinetics AT hoffmanndaniel bayesiandataintegrationquestionsclassicstudyonproteaseselfdigestkinetics |