Question #14 Amino acid mutations can in some cases dramatically alter proteinstructure and function. You are working in the lab and make a D to R mutation for a residue on.the surface of your favorite protein. PTP1B. What of the following possible effects would be mostlikely?APTP1B will become more stableBPTP1B will aggregate, since D is not hydrophobic but R is hydrophobic; thus ahydrophobic patch has been introduced on the protein surfacePTP1BS quaternary structure will changeD)PTP1B will elute earlier than it did before from an anion exchangechromatography columnOPTP1B will shift noticeably on an SDS-PAGE gel> 4)

the structure of the protein is determined by the charge of the amino acid.

Answered: Question #14. Amino acid mutations can…

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Question 4. Imagine the main chain of a protein bends back on itself so that two amino acid residues R1 and R2 come close to each other. In the table below are four possibilities for what R1 and R2 might be. In each case, decide whether a specific interaction could form between the residues. If a specific interaction could form, give the name of the interaction. R₁ cysteine tyrosine threonine arginine R₂ cysteine phenylalanine glutamine aspartate specific interaction? OO yes O yes O no no OO O yes no yes no name of specific interaction 0 П 0 0
Question 29 Which of the following statements is true regarding the formylmethionine that serves as the first amino acid in bacterial protein synthesis? A an aminoacyl-tRNA synthetase that is specific for formylmethionine attaches formylmethionine to the tRNA B the formyl group is removed during protein synthesis leaving methionine as the first residue in all bacterial proteins the formyl group donor is N¹0-formyl-tetrahydrofolate (D) the tRNA that carries formylmethionine is the same tRNA for methionine
Question 13 During elongation, TRNA binds initially to the A "P" site on the ribosome. B) any available site on A, or P or E c "A" site on the ribosome. D "E" site on the ribosome.
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 25 Calculate the net charges of the following peptides at pH 7.4. Indicate which amino acids bear chuarged side chans a) NH2-Asp-Leu-Phe-Ala-Lys-Pro-Glu-Gly-COOH b) NH2-GIn-Glu-Lys-Tyr-Trp-Arg-Ala-Leu-COOH DELL
QUESTION 13 You have isolated a nonsense mutation caused by a base substitution. This mutation is a null allele. You then use this mutant to select for second mutations that suppress the null phenotype back to a more wild-type phenotype. In theory, which of of the following types of second mutations are possible? A reverse mutation of the nonsense mutation A mutation in the anticodon of a tRNA gene precise deletion of the codon containing the nonsense mutation
Question 2. Ribosomes are cellular structures that are composed of protein and RNA; this structure is responsible for catalyzing peptide bond formation between amino acids during a process known as translation. a) Many antibiotics that kill bacteria target translation. Why might this be an effective mechanism to kill bacteria? Why don't antibiotics also kill human (eukaryotic) ribosomes? b) The antibiotic Kasugamycin (KSG) destabilizes the P-site of the ribosome. Describe what parts of translation would be altered in the presence of this antibiotic. c) How does the following graph show the efficacy of translational knockdown with KSG? Met-Methionine C % of Met incorporation 100 80 60 40 20 0 + 0 2 4 6 8 KSG concentration (mg/ml) 10
Question 16 What happens when a stop codon is reached by a ribosome? A termination tRNAter binds to the codon and the growing peptide is transferred to it. When the peptidyl-tRNAter A reaches the P site, the ribosome is signaled to release the protein. The ribosome then is likely to dissociate. A termination tRNAter binds to the codon and the growing peptide is transferred to it. When the peptidyl-tRNAter (B) reaches the P site, the ribosome dissociates. A separate peptidyl transferase then releases the protein from tRNAter. A termination tRNAter binds to the codon and is used to release the growing peptide from the P site TRNA. The ribosome then is likely to dissociate. D A release factor binds to the codon and is used to release the growing peptide from the P site tRNA.
QUESTION 46 Vancomycin and B-lactam antibiotics are similar in what way? OA. They both prevent NAM-NAG glycosdic bond formation in peptidoglycan OB. They both upregulate transpeptidase expression C. They both prevent peptide side chain cross-linking in peptidoglycan O D. They both contain beta lactam ring structures OE. They both cleave NAM-NAG glycosdic bonds in peptidoglycan
Question 5 (5 points) Match the following tripeptide with its given characteristic: contains sulfur? 1. Tyr-Lys-Met contains the largest number of nonpolar R groups? 2. Gly-Pro-Arg 3. Asp-Trp-Tyr contains two amino acids that contain aromatic ring? 4. Asp-His-Glu is known as glutathione? 5. Leu-Val-Phe is most negatively charged at pH 7? 6. Glu-Cys-Gly Identification
Question 3. An abnormally high levels intracellular tangles are observed to occur in the brains of patients suffering from several fatal neurodegenerative diseases like Alzheimer's disease. These tangles are composed of protein that has an unusually high level of which post-translational modification?
Question 5

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