Question 24 of 25Given the following reaction below, what amino acid is involved and what is the specific reaction that it undergoes?OHHistidinePhosphoamide formationPhenylalanineTyrosinePhosphodiester bond formationPhosphoester bond formationPhosphomethyl formationTryptophan0=P'-0"24

Phenylalanine, tyrosine, and tryptophan are aromatic amino acids. The side chain of the…

Answered: Given the following reaction below,…

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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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 22: which of the following secondary structures would you expect to find on the surface of a globular protein? Alpha helix Beta sheet Loops between two alpha-helices None of the above because water would disrupt the hydrogen bonding that stabilizes these structures A,B and C as long as the polar and charged amino acid side chains face the surface of the protein.
Question 1Predicting Secondary Structure Which of the following peptides is more likely to take up an -helical structure, and why? (a) LKAENDEAARAMSEA (b) CRAGGFPWDQPGTSN
QUESTION 22 When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Allosteric activation Zymogen activation Covalent modification Competitive inhibition Allosteric inhibition
QUESTION 16 Peptidyl transferase activity (peptide bond enzyme activity) is associated with what site in the ribosome? E P A X
Question 9. Which of thefollowing is not formed through adehydration synthesis reaction?A. polysaccharideB. polypeptideC. Nucleic acidD. phospholipidE. glycerol
Question 10. All of the following areparts of a nucleotide EXCEPT:A. a five-carbon sugar.B. a six-carbon sugar.C. a phosphate group.D. a nitrogenous base.
QUESTION 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-phosphate
question 38 The constant region of each heavy chain determines the class of the heavy chain. True False
Question 4. If you were to synthesize a tetrapeptide consisting of all alanine residues, you would have how many bonds between carbon and nitrogen?
QUESTION 5 [20]Describe and compare the metabolism of carbohydrates, lipids and proteins and in your answer, explain the role of ATP. Also discuss the differences between anabolic and catabolic pathways, the regulation of metabolic pathways and the differences in metabolism between the well-fed and 1.1 Describe the structural characteristics that are common to all the amino acids that are found in mammalian proteins and draw the structure of the tripeptide Tyr-Thr-Trp in the ionic form that predominates at pH 7. Show all atoms (including hydrogens) as well as any charges as necessary. Explain the general features of amino acid side chains and the importance of associated non-covalent interactions. (1fasting state.
QUESTION 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:

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Given the following reaction below, what amino acid is involved and what is the specific reaction that it undergoes? OH Histidine Phosphoamide formation Phenylalanine Tyrosine Phosphodiester bond formation Phosphoester bond formation Phosphomethyl formation Tryptophan O=P-