Which of the following is common among proteins with similar purification levels: Similar ________ Note: More than one answer may be correct A. Molecular weight B. Concentration C. Isoelectric Point D. Solubility E. Function. Explain your answer

This is a visible spectra between 390-590 nm obtained during the protein separation process of haemoglobin and cytochrome c using CM Sephadex chromatography. I'd like the results shown on the image interpreted. Look for characteristic peaks or patterns that correspond to the absorption properties of these proteins in the visible range.

There are 4 classes of biochemical families (Carbohydrates, Proteins, Lipids, and Nucleic Acids). Identify the biochemical family that is described by the statements below. 1. The monomer of this biochemical family is called an amino acid. 2. DNA is an example of this biochemical family. 3. Glucose and sucrose are an example of this biochemical family. 4. Vitamin A, steroids, waxes, and phospholipids are all examples of this biochemical family. 5. This diverse biochemical family is known for being nonpolar and insoluble in water. 6. This biochemical family is the genetic material in an organism and is made up of a phosphate, sugar, and base monomer. 7. The monomer of this biochemical family contains an amine and a carboxylic acid functional group. Two monomers are linked together through condensation polymerization of these two functional groups.

You have a soluble protein that is highly flexible and is only 23 kDa in size. What is the most suitable technique (X-ray crystallography, NMR, cryo-EM) for structure determination of this protein? Explain your reasoning.

Both milk and egg whites (albumin) contain proteins. What do your findings suggest for the stability of these proteins at higher temperature?

Mass spectrometry and X‑ray diffraction are common biochemical techniques for characterizing proteins. Classify each statement based on whether it applies to mass spectrometry, X‑ray diffraction, or both techniques.

detail how cation exchange chromatography works and what you would use to elute your target protein. What protein information would you need to facilitate this approach? Would you need to do any protein engineering to utilize cation exchange chromatography, justify your answer?

A mixture of two proteins (both with mass of 50 kDa) with an molecular isoelectric points of 7.8 and 8.9, respectively, is in a buffered solution at pH 7. Which type of liquid chromatography would be used to separate these two proteins? O a. O b. O C. d. e. anion exchange chromatography size-exclusion column gel filtration Ni-NTA column cation exchange chromatography

Proteins and Amino Acids A. Acid-base properties of proteins: 1. Data a. Color phenolphthalein-NaOH solution -before adding casein : colorless - after adding casein :colorless cloudy b. Color of methyl orange-HCl solution - before adding casein :Blue - after adding casein : Pink 2. Why did the solutions change color? 3. Which property of proteins is illustrated by the above? 4. Why as methyl orange used in place of phenolphthalein in the second part of this procedure? B. Isoelectric point of casein: 1. Data Initial pH of milk Final pH of milk 2. What is the isoelectric point of casein? C. Denaturation of proteins: A. pH 1. Observations: a. Tube no. 1: concentrated HCI b. Tube No. 2: concentrated HNO, c. Tube No. 2: concentrated H,SO, 2. Which structure(s) of the protein were disrupted in this procedure?

Discuss the mechanism that leads to aggregation of a protein therapeutic via a conformationally-altered monomer. Suggest one method of minimising aggregation via the mechanism above. please only answer if you are goin to explain well