1. Most pure proteins are insoluble in pure distilledwater but dissolve in dilute salt concentrations.However, the addition of high concentrations ofneutral salts to an aqueous solution of protein causesit to precipitate. Name this phenomenon and suggesta molecular explanation for the observation that highconcentrations of added salts decrease the solubilityof proteins.2. Capillary gel electrophoresis (CGE) forms part of afamily of related techniques that comprise capillaryelectrophoresis (CE). Give a brief description of thistechnique with particular reference to its separationcharacteristics and applications.

When a protein's ionic strength is low, its solubility rises as the salt concentration rises. The…

Answered: 1. Most pure proteins are insoluble in…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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5 You need to separate the following three proteins, Protein A (MW 76 600 Da; pI 4.5); Protein B (MW 70 000 Da and pI 8.2) and Protein C (MW 42 000; pI 8.6). Describe what column/s you would use, the pH of the buffer/s you would use, which proteins are retained on the column and how you would elute the bound protein/s. How would you monitor where the protein peaks elute and whether the protein in each peak is pure of not?
1. Discuss how the pH and temperature affect the solubility of protein. 2. Explain "salting-in" in your own words.
It is observed that as temperature is increased, most protein molecules gofrom their defined, folded state into a random-coil, denatured state thatexposes more hydrophobic surface area than is exposed in the folded state.(a) Given what you have learned so far about ΔH and ΔS, explain why thisis reasonable. (b) Sometimes, however, proteins denature as temperature is decreased.How might this be explained?
3. A biochemist purified a protein from the bloodstream and determined its molecular weight under several conditions. In 8 M urea, which denatures the polypeptide chain, the molecular weight of the protein was 150,000 Da. She found that under reducing conditions the molecular weight of the protein was 75,000 Da, while under oxidizing conditions the molecular weight of the protein was 150,000 Da. Explain these results.
3 i. Define Biological Value (BV) of Proteinsii. What are the advantages of this protein evaluation method when compared to Nbalance and chemical score?5iii. A bull consumes 7 kg DM of feed containing 60 g N/kg. The bull excretes 120 g N inthe faeces and 50 g N in the urine. The feacal and urinary N had 20 g metabolic feacalnitrogen (MFN) and 6 g endogenous urinary nitrogen (EUN) respectively.Calculate the BV of the protein in the diet.
Explain how tandem mass spectroscopy is used to determinethe sequence of a peptide. Once a peptide sequence is known,how is this information used to determine the sequence of theentire protein?
Residues such as valine, leucine, isoleucine, methionine, andphenylalanine are often found in the interior of proteins,whereas arginine, lysine, aspartic acid, and glutamic acid areoften found on the surface of proteins. Suggest a reason forthis observation. Where would you expect to find glutamine,glycine, and alanine?
1. What is hemoglobinopathy? What is sickle-cell anemia? Explain the concept relating to protein structure. 2. How does the oxygen-carrying functions of myoglobin differ from that of hemoglobin?
1. a. Explain why the melting point of palmitic acid (16 carbons, no double bonds) is slightly lower thanthat of stearic acid (18 carbons, no double bonds). Explain why the melting point of oleic acid (18carbons, one double bond) is lower than that of stearic acid b. A mixture of lipids containing phosphatidic acid, cholesterol, testosterone, phosphatidylserine, andphosphatidylethanolamine was applied to a hydrophobic interaction chromatography column. Thecolumn was washed with a high salt buffer, and the lipids were then eluted with decreasing saltconcentrations. In what order would the lipids be eluted from the column? Explain your answer.
The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.
a. Why proteins are extracted to a buffered solution? Briefly describe the components of ageneralized protein extraction buffer?.b. Describe the basis of affinity chromatography in protein purification.c. What is the most appropriate method of protein elution in affinity chromatography?d. List three examples of commonly employed combinations of ligand and protein in affinitychromatography.
A 20µL unknown protein was mixed with 80µL of water. Then, 10µL of this mixture was added with 10µL Bradford reagent and diluted with water to a total volume of 100µL. The absorbance at 595 nm shows 0.08 units. Solve for the protein concentration (in mg/mL) of the original unknown protein. How much protein (in mg) is in the 20uL sample? Express your answer in 3 significant figures.

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