Learning about protein solubility from bacterial inclusion bodies

doi:10.1186/1475-2859-8-4

Microbial Cell Factories

Volume 8

Viewing options:

Abstract
Full text
PDF (231KB)

Associated material:

Related literature:

Articles citing this article
on BioMed Central
on Google Scholar
on ISI Web of Science
on PubMed Central
Other articles by authors
on Google Scholar

Martínez-Alonso M
González-Montalbán N
García-Fruitós E
Villaverde A

on PubMed

Martínez-Alonso M
González-Montalbán N
García-Fruitós E
Villaverde A
Related articles/pages
on Google

on Google Scholar

on PubMed

Tools:

Post to:

Commentary

Learning about protein solubility from bacterial inclusion bodies

Mónica Martínez-Alonso¹^,2 , Nuria González-Montalbán¹^,2 , Elena García-Fruitós¹^,2 and Antonio Villaverde¹^,2

¹Institute for Biotechnology and Biomedicine and Department of Genetics and Microbiology, Autonomous University of Barcelona, Barcelona, Spain

²CIBER de Bioingeniería, Biomateriales y Nanomedicina (CIBER-BBN), Spain

author email corresponding author email

Microbial Cell Factories 2009, 8:4doi:10.1186/1475-2859-8-4


Published:	8 January 2009

Abstract

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.