Structural hot spots for the solubility of globular proteins

Structural hot spots for the solubility of globular proteins

Mutations in aggregation prone regions of recombinant proteins often improve their solubility, although they might cause negative effects on their structure and function. Here, the authors identify proteins hot spots that can be exploited to optimize solubility without compromising stability.

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Autores principales: Ashok Ganesan, Aleksandra Siekierska, Jacinte Beerten, Marijke Brams, Joost Van Durme, Greet De Baets, Rob Van der Kant, Rodrigo Gallardo, Meine Ramakers, Tobias Langenberg, Hannah Wilkinson, Frederik De Smet, Chris Ulens, Frederic Rousseau, Joost Schymkowitz
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2016
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Q
Acceso en línea:https://doaj.org/article/83b3c708399847f480f311a4edf53932
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spelling oai:doaj.org-article:83b3c708399847f480f311a4edf539322021-12-02T14:39:53ZStructural hot spots for the solubility of globular proteins10.1038/ncomms108162041-1723https://doaj.org/article/83b3c708399847f480f311a4edf539322016-02-01T00:00:00Zhttps://doi.org/10.1038/ncomms10816https://doaj.org/toc/2041-1723Mutations in aggregation prone regions of recombinant proteins often improve their solubility, although they might cause negative effects on their structure and function. Here, the authors identify proteins hot spots that can be exploited to optimize solubility without compromising stability.Ashok GanesanAleksandra SiekierskaJacinte BeertenMarijke BramsJoost Van DurmeGreet De BaetsRob Van der KantRodrigo GallardoMeine RamakersTobias LangenbergHannah WilkinsonFrederik De SmetChris UlensFrederic RousseauJoost SchymkowitzNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-15 (2016)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Ashok Ganesan
Aleksandra Siekierska
Jacinte Beerten
Marijke Brams
Joost Van Durme
Greet De Baets
Rob Van der Kant
Rodrigo Gallardo
Meine Ramakers
Tobias Langenberg
Hannah Wilkinson
Frederik De Smet
Chris Ulens
Frederic Rousseau
Joost Schymkowitz
Structural hot spots for the solubility of globular proteins
description Mutations in aggregation prone regions of recombinant proteins often improve their solubility, although they might cause negative effects on their structure and function. Here, the authors identify proteins hot spots that can be exploited to optimize solubility without compromising stability.
format article
author Ashok Ganesan
Aleksandra Siekierska
Jacinte Beerten
Marijke Brams
Joost Van Durme
Greet De Baets
Rob Van der Kant
Rodrigo Gallardo
Meine Ramakers
Tobias Langenberg
Hannah Wilkinson
Frederik De Smet
Chris Ulens
Frederic Rousseau
Joost Schymkowitz
author_facet Ashok Ganesan
Aleksandra Siekierska
Jacinte Beerten
Marijke Brams
Joost Van Durme
Greet De Baets
Rob Van der Kant
Rodrigo Gallardo
Meine Ramakers
Tobias Langenberg
Hannah Wilkinson
Frederik De Smet
Chris Ulens
Frederic Rousseau
Joost Schymkowitz
author_sort Ashok Ganesan
title Structural hot spots for the solubility of globular proteins
title_short Structural hot spots for the solubility of globular proteins
title_full Structural hot spots for the solubility of globular proteins
title_fullStr Structural hot spots for the solubility of globular proteins
title_full_unstemmed Structural hot spots for the solubility of globular proteins
title_sort structural hot spots for the solubility of globular proteins
publisher Nature Portfolio
publishDate 2016
url https://doaj.org/article/83b3c708399847f480f311a4edf53932
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