Computer simulations explain the anomalous temperature optimum in a cold-adapted enzyme

Enzymes from organisms inhabiting cold environments (psychrophiles) have adapted to catalyzing chemical reactions at near freezing temperatures. Here – using molecular dynamics simulations – the authors analyze cold adaptation of psychrophilic α-amylase and provide the structural basis for its low a...

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Autores principales:	Jaka Sočan, Miha Purg, Johan Åqvist
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/884691212e474ae6a75d5ebf6a689783
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id	oai:doaj.org-article:884691212e474ae6a75d5ebf6a689783
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spelling	oai:doaj.org-article:884691212e474ae6a75d5ebf6a6897832021-12-02T16:53:16ZComputer simulations explain the anomalous temperature optimum in a cold-adapted enzyme10.1038/s41467-020-16341-22041-1723https://doaj.org/article/884691212e474ae6a75d5ebf6a6897832020-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16341-2https://doaj.org/toc/2041-1723Enzymes from organisms inhabiting cold environments (psychrophiles) have adapted to catalyzing chemical reactions at near freezing temperatures. Here – using molecular dynamics simulations – the authors analyze cold adaptation of psychrophilic α-amylase and provide the structural basis for its low anomalous temperature optimum: the increased mobility of a surface loop involved in substrate interaction.Jaka SočanMiha PurgJohan ÅqvistNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jaka Sočan Miha Purg Johan Åqvist Computer simulations explain the anomalous temperature optimum in a cold-adapted enzyme
description	Enzymes from organisms inhabiting cold environments (psychrophiles) have adapted to catalyzing chemical reactions at near freezing temperatures. Here – using molecular dynamics simulations – the authors analyze cold adaptation of psychrophilic α-amylase and provide the structural basis for its low anomalous temperature optimum: the increased mobility of a surface loop involved in substrate interaction.
format	article
author	Jaka Sočan Miha Purg Johan Åqvist
author_facet	Jaka Sočan Miha Purg Johan Åqvist
author_sort	Jaka Sočan
title	Computer simulations explain the anomalous temperature optimum in a cold-adapted enzyme
title_short	Computer simulations explain the anomalous temperature optimum in a cold-adapted enzyme
title_full	Computer simulations explain the anomalous temperature optimum in a cold-adapted enzyme
title_fullStr	Computer simulations explain the anomalous temperature optimum in a cold-adapted enzyme
title_full_unstemmed	Computer simulations explain the anomalous temperature optimum in a cold-adapted enzyme
title_sort	computer simulations explain the anomalous temperature optimum in a cold-adapted enzyme
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/884691212e474ae6a75d5ebf6a689783
work_keys_str_mv	AT jakasocan computersimulationsexplaintheanomaloustemperatureoptimuminacoldadaptedenzyme AT mihapurg computersimulationsexplaintheanomaloustemperatureoptimuminacoldadaptedenzyme AT johanaqvist computersimulationsexplaintheanomaloustemperatureoptimuminacoldadaptedenzyme
_version_	1718382871393075200

Computer simulations explain the anomalous temperature optimum in a cold-adapted enzyme

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