1. In the Procedure, you were instructed to use your original mixture ofphycocyanin and 0.10 M sodium phosphate buffer as your reference solutionbecause the buffer stabilizes the protein in its native (folded) form. Brieflyexplain how the buffer stabilizes the phycocyanin.

Buffers are compounds that can resist changes in pH, allowing the protein to remain in its…

Answered: In the Procedure, you were instructed…

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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1. Why must the solution to be tested with ninhydrin be neutral? 2. Are Xanthoproteic and Millon Nasse tests satisfactory for use in the urinary examination for protein? Why? 3. Which test can be used to show up to what stage the hydrolysis of a protein proceeds? Why?
The elution of a protein with an isoelectric point of 7.5, is mostly likely to be affected by a change in pH from 7.4 to 6.9 in which type of protein separation technique? a.) size exclusion chromatography b.) SDS-acrylamide gel electrophoresis c.) affinity chromatography d.) ion exchange chromatography
Which of the following about protein denaturation is not trueA. It is always irreversible B. It is a shape change C. It may be due to pH / temperature change D. Most of the proteins denature when transferred from aqueous environment to organs solvents E. Its function is lost.
Suppose you have a cell-lysis sample containing genomic DNA, a complex mixture of proteins, and debris. Describe different commonly used analytical methods to i) analyze the molecular masses of the protein mixture. ii) detect the composition (what specific amino acids are there in what proportion) of a specific protein from the mixture. iii) deduce the sequence of some particular proteins from the mixture content
5. What will happen to a protein if subjected to high tempuraturea?
1. The hydropathic index represents the sum of hydrophobic and hydrophilic residues of a polypeptide. A.true B.false
1.Describe in detail how to detect the primary structure of protein. 2.Given a mixture of lysine,histidine and cysteine.The isoelectronic point of the amino acids are as follows: histidine:7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.
hoose the reagents that help unfold the protein molecules into same shape and charge density. a. beta-mercaptoethanol (β-ME) b. poly-acrylamide c. TEMED d. sodium-dodecyl-sulfate (SDS)
The rate of migration of a protein through an SDS-poly-acrylamide gel is NOT influenced by A. Strength of the electric field B. Size of the protein. C. Pore size of the gel. D. Charge of the protein.
1..Calculate the number of kcal and amount of protein provided by the following formula: 500 mL of 50% dextrose and 1 liter of a 10% amino acid solution. If 250 mL of a 20% intravenous fat emulsion were added, how many more kcal would be provided?
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?
Describe the 4 levels of protein structure: primary, secondary, tertiary and quaternary. And, note which will be disrupted by application of heat.

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In the Procedure, you were instructed to use your original mixture of phycocyanin and 0.10 M sodium phosphate buffer as your reference solution because the buffer stabilizes the protein in its native (folded) form. Briefly explain how the buffer stabilizes the phycocyanin.