Ontology highlight
ABSTRACT:
SUBMITTER: Castaldo C
PROVIDER: S-EPMC3744504 | biostudies-literature | 2013
REPOSITORIES: biostudies-literature
Castaldo Cristiana C Ciambellotti Silvia S de Pablo-Latorre Raquel R Lalli Daniela D Porcari Valentina V Turano Paola P
PloS one 20130815 8
Recombinant human Glutaminyl Cyclase expressed in E. coli is produced as inclusion bodies. Lack of glycosylation is the main origin of its accumulation in insoluble aggregates. Mutation of single isolated hydrophobic amino acids into negative amino acids was not able to circumvent inclusion bodies formation. On the contrary, substitution with carboxyl-terminal residues of two or three aromatic residues belonging to extended hydrophobic patches on the protein surface provided soluble but still ac ...[more]