Match the specificity pocket (identified by red number) to the residue that occupies it. 1 3 4 2 1. D 2. E 3. F 4. R 5. W 6. Y

4. a) The molecule below is a/n: amino acid dipeptide tripeptide (circle one) b) Would the molecule below test positive in the biuret test? Why/why not? If yes, label and point an arrow to the portion of the molecule responsible. H. H. NH3-C-C-NH-C-C CH3 CH2SH

Describe two different applications of superparamagnetic particles in bio-medicines and what are the advantages of using superparamagnetic particles.

I. Qualitative Analyses of Proteins Complete the table below. Chemical/reagent used (be specific) Final expected Test Sample Interpretation visible result after the experiment (color change, precipitation, etc.) Egg albumin Gelatin dispersion Biuret test 0.5% urea 0.5% glycine Egg albumin Xanthoproteic test Gelatin dispersion 0.5% lysine 0.5% tryptophan Egg albumin Gelatin dispersion 0.5% glycine 0.5% asparagine Egg albumin Ninhydrin test Millon's test Gelatin dispersion 0.5% tyrosine 0.5% glycine

You have a 50X stock solution of TAE buffer, but you need 2 L of a 1X solution for electrophoresis. How much stock should you use?

I want clear handwritten solution only....i will up vote

What can be the interpretation for the results given below? Test/s Results Ninhydrin Xanthroproteic Millon's + Biuret Pauly O The unknown sample contains tyrosine and tryptophan residues O The unknown sample only contains tyrosine as free amino acids The unknown sample contains tyrosine and histidine residues O The unknown sample contains tyrosine, tryptophan, and histidine residues

1. Why ninhydrin is used in paper chromatography?   2. How do you identify amino acids on the chromatogram?

Please answer part 4, 5 and 6.

Why is it important to be able to accurately measure protein content in a sample? For example, by using different methods such as colorimetric assays and UV assays.