Circular dichroism spectroscopy is used to analyze the secondary structure of Riboflavin Carrier Protein (RCP). Major secondary structure types, alpha-helices and beta-strands produce distinctive CD spectra. Secondary structure of unknown structure can be accessed from the known if unknown structure CD spectrum is given. We have observed the secondary structure of Riboflavin carrier protein contain of hen, coot and spotted owlet eggs white. Similar alpha percentage and beta stand percentage was observed in hen and coot but in spotted owlet Yolk difference in alpha percentage (%) and beta stand percentage (%) was seen. The secondary structure of RCP was estimated with an error of 0.32 using web base online K2D2 software. We have observed that this method improves the predictions of alpha and beta strand, particularly for the wavelength interval between 190 and 240 nm.