Lab #4: protein purification worksheet1.following ammonium sulfate precipitation and centrifugation what color is the pellet? what color is the supernatant? (1pt)2.our salt-precipitated protein (purple, red, or blue) will be re-dissolved in buffer that contains riboflavin (yellow) and passed over a desalting column. which color should come off the column first; the protein pigments or the yellow riboflavin? why? (1 pt)3.why is it important not to collect any yellow riboflavin along with the algal proteins? hint: what can happen during ion exchange chromatography you allowed your algal proteins to be contaminated with riboflavin? (1 pt)4.if a protein binds to the anion exchange resin at ph7, would you predict that they would also bind to the cation exchange resin at ph7? why or why not? (1 pt)5.which resin did you choose and which protein(s), phycoerythrin (red) and/or phycocyanin (blue), are bound to your resin? what does that tell you about their charge? (1 pt)