This is an SDS-PAGE gel of the protein insulin. The first lane is the molecular weight standard marker. The second lane NR is the native, non-reduced protein (MW 5.7kDa). The third lane is the protein treated with beta-mercaptoethanol. Please explain what is shown in the

I am not understanding why TA of alcohol precipitation is used as TA of purified protein. I provided 2 photos, 1 with the questions and the correct answer, and the other photo is a screenshot of the explanation.

Please type or write clear so I can see thanks

PLEASE have the following and help D:. What i need for the chosen of 2/3 choices.  2)   Illustrate detailed chemical scheme for how you will functionalize your biomolecule to the surface of the sensor (e.g. if you wanted to functionalize a protein to a gold SPR chip, you should could show the assembly of an amine-terminated SAM, followed by carbodiimide coupling of. the protein). These schemes should be drawn using a chemical illustration software package (ChemDraw / ChemSketch).Your chemical schemes should be as detailed as necessary to accurately depict the chemical design of your system, DO NOT INCLUDE a step-wise mechanism, it is not necessary. You should include at least one literature reference to support your conjugation strategy.3)  Include an illustration of the functional sensor, and describe whether the sensor is label-free or not, what signal is observed, and how you would detect the interaction (i.e. if a labeled antibody is required, you should describe what label would…

You are analyzing the peptide ala-ile-glu-lys-phe-val- tyr-cys. If you treat the peptide with chymotrypsin, which technique would be best to separate the fragments? O a. ultracentrifugation O b. affinity chromatography O c. dialysis d. gel filtration chromatography O e. ion exchange chromatography What is an advantage of NMR spectroscopy over x-ray crystallography in studying protein structure?

Briefly discuss how sickle cell mutation affects the protein.

Explain the Rf value obtained on the basis of the structure of amino acids use. Explain in 1-3 sentence only.

A purified protein fraction has a total sample volume of 360 µL.  The sample has a corrected A280 of 0.484, and the blank corrected A280 was 0.052.  (Both values were measured with a path length of 1.00 cm.)  If 5.00 µL of the sample was used in a reaction, calculate the mass of protein in the reaction (in µg).