a. Draw a PEC diagram that represents the relative potential energy and number of configurations for the unfolded and folded protein.
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- 5. What will happen to a protein if subjected to high tempuraturea?1. The antibiotics puromycin and erythromycin are known inhibitors of protein synthesis. (a) Which part of the protein synthesis is affected by each antibiotic? (b) What could be the reason why one of them is more effective than the other one when they are given in the same dose?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.
- 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.2. a. How do the majority of proteins that exist outside cells get outside cells? Explain the pathway. b. Explain at least three major exceptions to your answer in part a.2 If a protein is predominantly made up of aliphatic and aromatic amino acids, which of the following is most likely true about such protein? Select the correct responses): a. It is a protein with a net negative charge b. It is most probably a structural protein. c. It is a protein that is cationic in nature. d. It is a protein that is hydrophobic in nature. e. It is most probably a catalytic protein. f. It is a water-solube protein. g. It is most probably a carrier protein.
- 3. Why do we need to study the four levels of protein structure? Cite its practical use to our day-to-day life.1. What determines the affinity of a glycan for a GBP?2. Would you expect an instrinsically disordered protein to contain a higher proportion of hydrophilic or hydrophobic residues? Explain your reasoning.
- 1) What are the four levels of protein folding. How do you distinguish those different levels? What can denature a protein? 2) What are detergents and why are they useful? How do they basically work? 3) What is meant by amphipathic? What is an example of this?The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices unwind. c. sheet structures unfold. d. tertiary structure is changed. e. quaternary structures disassemble.1.Describe in detail how to determine the primary structure of protein. 2.You have been given a mixture of lysine, histidine and cysteine.The isoelectric 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.