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Learning about protein solubility from bacterial inclusion bodies
The progressive solving of the conformation of aggregated proteins and the conceptual understanding of the biology of inclusion bodies in recombinant bacteria is providing exciting insights on protein folding and quality. Interestingly, newest data also show an unexpected functional and structural c...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2630952/ https://www.ncbi.nlm.nih.gov/pubmed/19133126 http://dx.doi.org/10.1186/1475-2859-8-4 |
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author | Martínez-Alonso, Mónica González-Montalbán, Nuria García-Fruitós, Elena Villaverde, Antonio |
author_facet | Martínez-Alonso, Mónica González-Montalbán, Nuria García-Fruitós, Elena Villaverde, Antonio |
author_sort | Martínez-Alonso, Mónica |
collection | PubMed |
description | The progressive solving of the conformation of aggregated proteins and the conceptual understanding of the biology of inclusion bodies in recombinant bacteria is providing exciting insights on protein folding and quality. Interestingly, newest data also show an unexpected functional and structural complexity of soluble recombinant protein species and picture the whole bacterial cell factory scenario as more intricate than formerly believed. |
format | Text |
id | pubmed-2630952 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-26309522009-01-27 Learning about protein solubility from bacterial inclusion bodies Martínez-Alonso, Mónica González-Montalbán, Nuria García-Fruitós, Elena Villaverde, Antonio Microb Cell Fact Commentary The progressive solving of the conformation of aggregated proteins and the conceptual understanding of the biology of inclusion bodies in recombinant bacteria is providing exciting insights on protein folding and quality. Interestingly, newest data also show an unexpected functional and structural complexity of soluble recombinant protein species and picture the whole bacterial cell factory scenario as more intricate than formerly believed. BioMed Central 2009-01-08 /pmc/articles/PMC2630952/ /pubmed/19133126 http://dx.doi.org/10.1186/1475-2859-8-4 Text en Copyright © 2009 Martínez-Alonso et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Commentary Martínez-Alonso, Mónica González-Montalbán, Nuria García-Fruitós, Elena Villaverde, Antonio Learning about protein solubility from bacterial inclusion bodies |
title | Learning about protein solubility from bacterial inclusion bodies |
title_full | Learning about protein solubility from bacterial inclusion bodies |
title_fullStr | Learning about protein solubility from bacterial inclusion bodies |
title_full_unstemmed | Learning about protein solubility from bacterial inclusion bodies |
title_short | Learning about protein solubility from bacterial inclusion bodies |
title_sort | learning about protein solubility from bacterial inclusion bodies |
topic | Commentary |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2630952/ https://www.ncbi.nlm.nih.gov/pubmed/19133126 http://dx.doi.org/10.1186/1475-2859-8-4 |
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