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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...

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Detalles Bibliográficos
Autores principales: Rojek, Marcin J., Walt, David R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
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.
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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
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