12) Which of the following types of enzyme carries out phosphorylation of a protein?
(a) isomerase
(b) kinase
(c) phosphodiesterase
(d) lyase
(e) hydrolase
13) Flavin adenine nucleotide is a coenzyme for which of the following?
(a) monoamine oxidase
(b) trypsin
(c) chymotrypsin
(d) Na+ K+ ATPase
(e) all of the above
14) A noncompetitive inhibitor
(a) binds only to [ES]
(b) binds either [E] or [ES]
(c) binds only to [E]
(d) binds only to [S]
(15) Which of the following is least likely to be found covalently attached in an amino acid building block used for proteins?
(16) Which of the following groups of amino acids all have aromatic R groups?
(17) Which of the following amino acids are all basic in a solution of pH 7.0?
(18) alpha helix is abundant in which of the following
19) A prosthetic group is ?
(a) a repair enzyme
(b) a non-amino acid group that is part of an enzyme
(c) a particular amino acid that is part of an enzyme
(d) a group that generates the native form of a protein
(e) a group that reduces enzyme activity
20) Which level of protein structure is most important in the positioning of an enzyme’s active site residues for substrate binding?
(a) primary structure
(b) secondary structure
(c) tertiary structure
(d) quatenary structure
21) Which of the following is true for the effects of a competitive inhibitor on an enzyme?
(b) Km is increased and Vm stays the same
(c) Km stays the same and Vm is increased
(d) Km stays the same and Vm is decreased
(e) Km and Vm are increased
12. b) Kinase
13. a) monoamine oxidase
14. b) binds either [E] or [ES].
15. e) all of the above.
16. e) all of the above.
17. b) lys and arg
18. a) hemoglobin only.
19. b) a non amino acid group that is part of an enzyme.
20. a) primary structure.
21. d) Km is increased and Vm stays the same.
12) Which of the following types of enzyme carries out phosphorylation of a protein? (a) isomerase...
Namer A) alternating sugar and nitrogen bases liked by peptide bonds B) complimentary bases held together by hydrogen bonds 6) The backbone of a niacleic acid strand consists of: alternating sugar and phosphate groups linked by phosphate ester bonds D) alternating nitrogen bases and phosphate groups linked by amide bonds Q 7) 刁what amino acids are involved in the following tripeptide? NH-CH-C-NH-CH-- CH NH OH D) His-Lys-Phe A) Tyr-His-Lys C) Lys-His-Tyr B) Lys-His-Phe 8) Which list contains only neutral polar...
Question 13 0.5 pts Protein phosphorylation is catalyzed by? Protein kinase Protein Phosphatase Antibodies Antigens None of the above Question 14 0.5 pts In an aqueous solution, which amino acid will orient itself inside the center of the protein? Valine Aspartic Acid Arginine Serine Glutamine Question 15 0.5 pts Enzymes in the enzyme class "kinase": Break down nucleic acids by hydrolying bonds between nucleotides O Catalyze the addition of phosphate groups to molecules Break down proteins by hydrolyzing peptide bonds...
please help with these 5 questions Consider a polypeptide consisting of 19 amino acid residues. Its structure is shown below. Lys-Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln-Tyr . Draw the fragments that would result if the peptide was treated with trypsin. (No partial credit) . Draw the fragments that would result if the peptide was treated with chymotropsin. (No partial credit) MATCH a term from the list below to each definition. Place the letter of the term in the blank to the left of the definition...
20. Protein amino acid side chains can hydrogen bond in the major groove of DNA, and discriminate between each of the four possible base pairs. In which one of the following groups of amino acids can all three members potentially be used in such DNA-protein recognition? A) Ala, Asn, Glu B) Arg. Gin, Leu C) Asn, Gin, Trp D) Asn, Glu, Lys E) Glu, Lys, Pro 21. Compared with DNA polymerase, reverse transcriptase: A) does not require a primer to...
41. An enzyme-substrate complex forms when substrate binds to an enzyme at the enzyme's site. 42. An inorganic ion such as zinc or manganese that is needed for an enzyme to function is acting as a 43. Competitive inhibition of enzymes occurs when: site A) catalytic B) allosterie C) operative B) cofactor C) apoenzyme D) holoenzyme A) coenzyme A) the inhibitor binds to the active site of the enzyme B) the inhibitor binds to the allosteric site of the enzyme...
4. The protein shown below is an enzyme-linked receptor. This means that this protein... Circle your answer a) can speed up chemical reactions. b) can bind to certain signaling molecules. c) all of the above. D. Think about the enzyme-linked receptor we discussed in class. After the signaling molecules binds to this receptor, it causes the active site on the receptor to become available. What binds to this active site? E. Consider the molecule you named in the previous question....
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and KM values are shown below for enzyme-substrate pairs. Which of the following enzymes is most efficient in converting the substrate into the product? b) kes.-4x10s s", KM-0.026 M d)k,,-5.7 x1o's", K-2x10s M c)人at-900 s", KM-2.5 × 10.5 M A2. Which of the following enzyme reaction mechanisms has multiple substrates? a) induced-fit e) Michaclis-Menton b) random sequential d) reversible covalent modification e) None...
repulsion within the protein 10. Which of the following amino acids do not contain a chiral carbon? a. Proline b. Alanine c. Glycine d. Phenylalanine e. Tyrosine 11. You want to determine an amino acid sequence for a particular polypeptide. So you degrade the peptid and get the following fragments. Determine the peptide sequence. Digested with typsin: Met-Val-Ser-Thr-Lys Val-lle-Trp-Thr-Leu-Met-lle Leu-Phe-Asn-Glu-Ser-Arg Digested with chymotrypsin: Asn-Glu-Ser-Arg-Val-lle-Trp Thr-Leu-Met-lle Met-Val-Ser-Thr-Lys-Leu-Phe a. Val-lle-Trp-Thr-Leu-Met-lle-Leu-Phe-Asn-Glu-Ser-Arg-Met-Val-Ser-Thr-Lys b. Val-lle-Trp-Thr-Leu-Met-lle-Met-Val-Ser-Thr-Lys-Leu-Phe-Asn-Glu-Ser-Arg c. Leu-Phe-Asn-Glu-Ser-Arg-Met-Val-Ser-Thr-Lys-Val-lle-Trp-Thr-Leu-Met-le d. Met-Val-Ser-Thr-Lys-Leu-Phe-Asn-Glu-Ser-Arg-Val-le-Trp-Thr-Leu-Met-lle e. Met-Val-Ser-Thr-Lys-Val-lle-Trp-Thr-Leu-Met-lle-Leu-Phe-Asn-Glu-Ser-Arg
PLEASE HELP OCHEM QUESTION 1. In the following protein, identify the type of bonding or interaction that is responsible for holding the two peptide chains together at each amino acid pair, above (A) and below (B). Gly - Ala - Ser - Cys - Val - Asp - Leu - Thr - His - Ile-Tyr-Glu - Phe - Lys - Cys - Met - Asn Val - Leu -Gin-Cys - Pro-Lys - Met - Tyr - Asp -Phe-Asn-Lys - Ile...
Which is the most inappropriate description of enzyme inhibition? Select one: a. A competitive inhibitor increases Km only. b. A noncompetitive inhibitor decreases Vmax only. c. An uncompetitive inhibitor decreases both Km and Vmax. d. All of the above e. None of the above