2. As we've seen previously, peptide bonds involving the amino acid proline can populate both "trans"and "cis" isomers.trans-Procis-ProThis isomerization reaction can be the rate-limiting step in protein folding. Depending on the proteinsequence, the relative favorability of the trans and cis states can change. For Pro-117 in the proteinstaphylococcal nuclease, the rates of the forward and reverse reactions are: ktrans→cis = 3.1 × 10-2and kcis→trans = 2.5 x 10-3 s-1.(a) What is AG°' for this reaction?(b) A prolyl isomeriase enzyme increases the rate of the forward reaction to kcat.trans->cis = 2.6 s-1.What is the new rate constant for the reverse reaction (kcat,cis→trans)?(c) This prolyl isomerase is a Michaelis-Menten enzyme with kcat = 2.6 s!, KM = 1.9 µuM. Ifyou have 1 nM enzyme, what is Vo for [S]o = 0.7 µM? What about [S]o = 30 µM? For eachcondition, what limits the reaction speed?

Michaelis-Menten model of enzyme kinetics is a very useful model which describe the relationship…

Answered: 2. As we've seen previously, peptide…

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter15: From Dna To Protein

Section: Chapter Questions

Problem 4TYK

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2. A mixture of the following amino acids (glu, leu, val, arg, ser, phe) was obtained upon complete hydrolysis of a hexapeptide. a. Edman’s reagent releases leucine b. Hexapeptide with carboxypeptidase releases serine. c. Hexapeptide with trypsin forms a tripeptide A with leucine at the N terminal and tripeptide B with valine at the N terminal. d. Tripeptide A with carboxypeptidase releases arginine and a dipeptide with glutamic acid at C terminal. e. Tripeptide B with chymotrypsin form releases serine and another dipeptide. Give: 1. the amino acid sequence of tripeptide A and B. 2. the amino acid sequence in the above hexapeptide.
1. What is the length in AA’s of the LilP protein? Assume fMet is NOT CLEAVED. 2. Write out the sequence of the polypeptide in AA: use the three letter notation, e.g. Met-Ser-Pro-
1. What is the isoelectric point (pI) of lysine which has pKa values of 2.1 for the α carboxyl group, 9.7 for the α amino group and 10.5 for the side chain amino group? 2. Which of the following is most likely to be found on the exterior of a protein? A) Pro B) Trp C) Ser D) Glu 3. The type of reaction that forms a peptide bond is A) Elimination B) Hydrolysis C) Nucleophilic substitution D) Condensation
1. The figure above shows some of the more common modifications, such as phosphorylation (1), acetylation or methylation (2), adding sugars or lipids (3,4), or adding another polypeptide (5). There are many other possibilities as well.Find and label each of these on the diagram. How might these modifications affect the protein?
3. In studying normal and mutant forms of a particularhuman enzyme, a geneticist came across a particularly interesting mutant form of the enzyme. Thenormal enzyme is 227 amino acids long, but themutant form was 312 amino acids long. The extra85 amino acids occurred as a block in the middleof the normal sequence. The inserted amino acidsdo not correspond in any way to the normal proteinsequence. What are possible explanations forthis phenomenon? How would you distinguishamong them?
8. List 4 tertiary interactions that exist in protein molecules and include what type of R groups (side chains) that must be present to undergo that specific interation.
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?
6. Please describe the events that may result in a mature protein not having methionine asthe N-terminal amino acid.
1. What are the effects of a) amino acid composition and sequence and b) intramolecular and intermolecular forces of attraction to protein folding? 2. What molecular property of amino acids can be used to justity the concept that the "molecular part of the protein can exhibit the same property as the molecular 'whole' (protein molecule?). Provide a comprehensive discussion using one molecular property. 3. Discuss two metabolic disorders which are caused by protein misfolding. Explain the metabolic consequence of the disorder. 4. If a non-science person asks you what protein folding is and how the concept is related to metabolic disorders, how are you going to explain the concept? (please summarize the concepts used, thank you!)
1. Which of the following forms of lysine would you expect to predominate at low pH, neutral pH and high pH? 2. One of the 20 amino acids is unusual in that its side chain contains a ring that incorporates the amine functional group of the amino acid. What is the name of this amino acid? Write the chemical structure of this amino acid at physiological pH.
1. What determines the affinity of a glycan for a GBP?
4. Which best describes the contribution of quaternary (4’) structure of polypeptides to the native conformation of proteins: a) Structure that results from intrachain interactions of amino B) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence acid side chains of amino acids from beginning to end of molecule

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