About: SUMO fusion technology for difficult-to-express proteins

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	SUMO fusion technology for difficult-to-express proteins
Creator	Hall, John Mattern, Michael Butt, Tauseef Edavettal, Suzanne
source	PMC
abstract	The demands of structural and functional genomics for large quantities of soluble, properly folded proteins in heterologous hosts have been aided by advancements in the field of protein production and purification. Escherichia coli, the preferred host for recombinant protein expression, presents many challenges which must be surmounted in order to over-express heterologous proteins. These challenges include the proteolytic degradation of target proteins, protein misfolding, poor solubility, and the necessity for good purification methodologies. Gene fusion technologies have been able to improve heterologous expression by overcoming many of these challenges. The ability of gene fusions to improve expression, solubility, purification, and decrease proteolytic degradation will be discussed in this review. The main disadvantage, cleaving the protein fusion, will also be addressed. Focus will be given to the newly described SUMO fusion system and the improvements that this technology has advanced over traditional gene fusion systems.
has issue date	2005-04-09(xsd:dateTime)
bibo:doi	10.1016/j.pep.2005.03.016
bibo:pmid	16084395
has license	no-cc
schema:url	https://doi.org/10.1016/j.pep.2005.03.016
resource representing a document's title	SUMO fusion technology for difficult-to-express proteins
has PubMed Central identifier	PMC7129290
has PubMed identifier	16084395
schema:publication	Protein Expr Purif
resource representing a document's body	covid:PMC7129290#body_text
is schema:about of	named entity 'β-mercaptoethanol' named entity 'N-terminal' named entity 'eukaryotic' named entity 'compartmentalization' named entity 'protease' »more»

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