Selection for Soluble Proteins via Fusion with Chloramphenicol Acetyltransferase

AbstractThe low solubility of a protein is one of the most frequent impediments for its structural and functional analysis and, on a more practical aspect, for its application as an industrial enzyme. The reason for low solubility can lie in low conformational stability (1), in a high number of surface-exposed hydrophobic amino acids (2) or in certain structural features, such as membrane binding regions (3). By changing the amino acid sequence of these proteins, their solubility can be significantly improved (4,5). Hence a general method that can efficiently identify (i.e., select) more soluble protein variants from a large repertoire is very useful in evolving such proteins. KeywordsFusion ConstructChloramphenicol AcetyltransferaseResistance AnalysisTerrific Broth MediumSoluble VariantThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.