Fig. 1
From: A conserved odorant binding protein is required for essential amino acid detection in Drosophila
Molecular characterization of recombinant OBP19b. a SDS-PAGE analysis of purified OBP19b. Proteins were stained using Coomassie Brilliant Blue. The MW lane shows the molecular weight standard 6.5–26.6 kDa (Ultra-Low Range marker, Sigma-Aldrich). b MALDI-ToF mass spectrometry analysis of OBP19b. c Characterization of OBP19b folding based on circular dichroism spectroscopy. Far-UV circular dichroism spectrum of OBP19b. The protein concentration was 5.0 mg/mL in 50 mM sodium phosphate at pH 7.5.
