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Observing Single Enzyme Molecules Interconvert between Activity States upon Heating
In this paper, we demonstrate that single enzyme molecules of β-galactosidase interconvert between different activity states upon exposure to short pulses of heat. We show that these changes in activity are the result of different enzyme conformations. Hundreds of single β-galactosidase molecules ar...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3897666/ https://www.ncbi.nlm.nih.gov/pubmed/24465972 http://dx.doi.org/10.1371/journal.pone.0086224 |
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author | Rojek, Marcin J. Walt, David R. |
author_facet | Rojek, Marcin J. Walt, David R. |
author_sort | Rojek, Marcin J. |
collection | PubMed |
description | In this paper, we demonstrate that single enzyme molecules of β-galactosidase interconvert between different activity states upon exposure to short pulses of heat. We show that these changes in activity are the result of different enzyme conformations. Hundreds of single β-galactosidase molecules are trapped in femtoliter reaction chambers and the individual enzymes are subjected to short heating pulses. When heating pulses are introduced into the system, the enzyme molecules switch between different activity states. Furthermore, we observe that the changes in activity are random and do not correlate with the enzyme's original activity. This study demonstrates that different stable conformations play an important role in the static heterogeneity reported previously, resulting in distinct long-lived activity states of enzyme molecules in a population. |
format | Online Article Text |
id | pubmed-3897666 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-38976662014-01-24 Observing Single Enzyme Molecules Interconvert between Activity States upon Heating Rojek, Marcin J. Walt, David R. PLoS One Research Article In this paper, we demonstrate that single enzyme molecules of β-galactosidase interconvert between different activity states upon exposure to short pulses of heat. We show that these changes in activity are the result of different enzyme conformations. Hundreds of single β-galactosidase molecules are trapped in femtoliter reaction chambers and the individual enzymes are subjected to short heating pulses. When heating pulses are introduced into the system, the enzyme molecules switch between different activity states. Furthermore, we observe that the changes in activity are random and do not correlate with the enzyme's original activity. This study demonstrates that different stable conformations play an important role in the static heterogeneity reported previously, resulting in distinct long-lived activity states of enzyme molecules in a population. Public Library of Science 2014-01-21 /pmc/articles/PMC3897666/ /pubmed/24465972 http://dx.doi.org/10.1371/journal.pone.0086224 Text en © 2014 Rojek, Walt http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Rojek, Marcin J. Walt, David R. Observing Single Enzyme Molecules Interconvert between Activity States upon Heating |
title | Observing Single Enzyme Molecules Interconvert between Activity States upon Heating |
title_full | Observing Single Enzyme Molecules Interconvert between Activity States upon Heating |
title_fullStr | Observing Single Enzyme Molecules Interconvert between Activity States upon Heating |
title_full_unstemmed | Observing Single Enzyme Molecules Interconvert between Activity States upon Heating |
title_short | Observing Single Enzyme Molecules Interconvert between Activity States upon Heating |
title_sort | observing single enzyme molecules interconvert between activity states upon heating |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3897666/ https://www.ncbi.nlm.nih.gov/pubmed/24465972 http://dx.doi.org/10.1371/journal.pone.0086224 |
work_keys_str_mv | AT rojekmarcinj observingsingleenzymemoleculesinterconvertbetweenactivitystatesuponheating AT waltdavidr observingsingleenzymemoleculesinterconvertbetweenactivitystatesuponheating |