Expression and purification of Drosophila OBP44a with the aids of LC-MS and NMR.

ABSTRACT: The production of highly purified native soluble proteins in large quantities is crucial for studying protein structure and function. Odorant binding proteins (OBPs) are small, soluble, extracellular proteins with multiple disulfide bonds, whose functions include, but are not limited to, binding hydrophobic molecules and delivering them to their corresponding receptors expressed on insect olfactory receptor neurons. Expression of proteins with multiple disulfide bonds like OBPs usually results in insolubility and low yield, which has been a significant barrier to understanding their biological roles and physiological functions. In the E. coli system, expression of OBPs often results in insoluble inclusion bodies or a limited amount of periplasmic soluble proteins. Although expression of OB

SUBMITTER: He Y 

PROVIDER: S-EPMC10557525 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature