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- QUESTION NO. 1Targeting a protein to be degraded within proteasomes usually requires ubiquitin. In the function of ubiquitin all of the following are true except: A. ATP is required for activation of ubiquicin. B. a peptide bond forms between the carboxyl terminal of ubiquitin and an ε-amino group of a lysine . C. linkage of a protein to ubiquitin does not always mark it for degradation. D. the N-terminal amino acid is one determinant of selection for degradation. E. ATP is required by the enzyme that transfers the ubiquitin to the protein to be degraded QUESTION NO. 2Much of procollagen formation occurs in the endoplasmic reticulum and Golgi apparatus which requires signal peptide. All of the following statements about targeting a protein for the ER are true except. A. signal peptide usually has a positively charged N-terminus and a stretch of hydrophobic amino acids. B. signal peptide emerging from a free ribosome binds signal recognition…Question 1Predicting Secondary Structure Which of the following peptides is more likely to take up an -helical structure, and why? (a) LKAENDEAARAMSEA (b) CRAGGFPWDQPGTSNQuestion 11. // Hint: Isoelectric focusing separates proteins based on their pI values, and can separate proteins that only differ by a net charge of ±1.±1. Recall that an amino acid residue with a negatively charged R group has a relatively low isoelectric point (pI) where it has zero net charge. Likewise, an amino acid residue with a positively charged R group has a relatively high isoelectric point (pI) where it has zero net charge. Order from Low pH to High pH
- Question 1: tRNA and amino acyl tRNA synthetases Part g: What chemical and structural characters are shared by the amino acids Ile, Val and Met? Part h: What enzyme attaches Ile to tRNA? Part i: Compare the frequency of the correct Ile entering the active site and the frequency of an incorrect amino acid entering the active site of this enzyme. Be specific with numbers. Part j: Compare the frequency of the correct tRNA(Ile) entering the active site and the frequency of an incorrect tRNA entering the active site of this enzyme. Be specific with numbers. Part k: Apply the Entropy change formula and multiply by T = 303 K (30 C) to determine the energetic cost of accurately attaching Ile to its cognate tRNA(Ile). Part l: Is there enough energy in the chemical transformation of ATP → AMP + 2Pi to pay this information cost?Question 15 Activities found in the rough ER and its functions include the folllowing EXCEPT provides a membrane binding site for the RNA with signal a signal sequence facilitates post-translational modifications allows the entry of polypeptides that will undergo glycosylation provides a membrane scaffold for binding of ribosomes for protein synthesisQuestion 1: tRNA and amino acyl tRNA synthetases Part a: How many codons encode the amino acid Isoleucine (Ile, I)? Part b: How many codons encode the amino acid Valine (Val, V)? Part c: How many codons encode the amino acid Methionine (Met, M)? Part d: How many tRNAs decode the Ile codons? Part e: How many tRNAs decode the Val codons? Part f: How many tRNAs decode the Met codon?
- Question: A decapeptide composed of ser, ala, IIe. his, trp, phe was treated with 1-flouro- 2,4-dinitrobenzene. It gave a DNP-his on the N terminal and free trp when treated with carboxypeptidase. Upon partial hydrolysis of the peptide, the following fragments were obtained. a. his-lle-phe-ala c. his-ala-phe e. ser-lle-his b. ala-phe-trp d. phe-ala-ser Give the amino acid sequence of the above decapeptide.Question 10 (2 points) A protein heterodimer would be considered an example of: -primary structure -secondary structure -tertiary structure -quaternary structure -atomic structureQuestion 1: Your research project is concerned with the expression and purification of a protein called aldehyde dehydrogenase. Describe in detail all steps required from gene amplification to characterisation of the purified protein.
- Text:QUESTION 16 Protein maturation in the ER includes. A Disulfide bond formation B. proteolytic cleavage C attachment of oligosaccharide d. Prolyl isomertzationQUESTION NO.1which of the following are chemical characteristics of monosaccharides? A. They contain multiple hydroxyl groupsB. they contain an aldehyde or ketone group C. They contain a branching carbon backbone D. They contain a carbon-carbon double bond E. Every carbon in a monosaccharide is fully reduced F. Every carbon in a monosaccharide is a chiral centerQUESTION NO.2 glucose absorption is hindered by _________ deficiency A. Retinol B. Thiamine C. Potassium D. Sodium E. Ascorbic acid F. Calciferol QUESTION NO.3 phospholipids is made primarily from A. L-glycerol 1-phosphate B. L-glycerol 3-phosphate C. D-glycerol 3-phosphate D. -glycerol 1-phosphate E. sn-glycerol 1-phosphate F. sn-glycerol 3-phosphateQUESTION 6 What is the three ketter code for each peptide(a) KFYV(b) ERSC(c) PIMFThe 3-letter code for Peptide (a) is: The 3-letter code for Peptide (b) is: The 3-letter code for Peptide (c) is: