BIOCHEMISTRY (LOOSELEAF) >CUSTOM PKG<
8th Edition
ISBN: 9781305760738
Author: Campbell
Publisher: CENGAGE C
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 3, Problem 21RE
REFECT AND APPLY Consider the following peptides:
Expert Solution & Answer
Trending nowThis is a popular solution!
Students have asked these similar questions
The preferred substrate is T because the enzyme half-saturates at 7.00 mM for T, but requires 28.0 mM for U, and 112 mM for S.
b
Question Content Area
The rate constant k 2 with substrate S is 9.60×107 sec-1, with substrate T, k 2 = 6.00×104 sec-1, and with substrate U, k 2 = 2.40×106 sec-1.
Calculate the catalytic efficiency with S, T, and U.
Catalytic efficiency with S =
Catalytic efficiency with T =
Catalytic efficiency with U =
Does enzyme A use substrate S, substrate T, or substrate U with greater catalytic efficiency?
Fumerase catalyzes the conversion of fumerate to malate.
fumerate + H2O ⇋ malate
The turnover number, kcat, for fumerase is 8.00×102 sec-1. The Km of this enzyme for fumerate is 5.00×10-3 μmol mL-1.
a
In an experiment using 2.00×10-3 μmol·mL-1, what is Vmax?
Suppose you wanted to make a buffer of exactly pH 7.00 using KH2PO4 and Na2HPO4. If the final solution was 0.18 M in KH2PO4, you would need 0.25 M Na2HPO4. Now assume you wish to make a buffer at the same pH, using the same substances, but want the total phosphate molarity ([HPO42−]+[H2PO−4]) to equal 0.20 M. What concentration of the Na2HPO4 would be required?
Chapter 3 Solutions
BIOCHEMISTRY (LOOSELEAF) >CUSTOM PKG<
Ch. 3 - RECALL How do D-amino acids differ from L-amino...Ch. 3 - RECALL Which amino acid is technically not an...Ch. 3 - RECALL For each of the following, name an amino...Ch. 3 - RECALL Identify the polar amino acids, the...Ch. 3 - RECALL Identify the nonpolar amino acids and the...Ch. 3 - RECALL Are amino acids other than the usual 20...Ch. 3 - MATHEMATICAL Predict the predominant ionized forms...Ch. 3 - MATHEMATICAL Draw structures of the following...Ch. 3 - MATHEMATICAL Predict the predominant forms of the...Ch. 3 - MATHEMATICAL Calculate the isoelectric point of...
Ch. 3 - MATHEMATICAL Sketch a titration curve for the...Ch. 3 - MATHEMATICAL Sketch a titration curve for the...Ch. 3 - MATHEMATICAL An organic chemist is generally happy...Ch. 3 - MATHEMATICAL Sketch a titration curve for aspartic...Ch. 3 - REFECT AND APPLY Suggest a reason why amino acids...Ch. 3 - REFECT AND APPLY Write equations to show the ionic...Ch. 3 - REFECT AND APPLY Based on the information in Table...Ch. 3 - REFECT AND APPLY If you were to have a mythical...Ch. 3 - REFECT AND APPLY What would be the pI for the...Ch. 3 - REFECT AND APPLY Identify the charged groups in...Ch. 3 - REFECT AND APPLY Consider the following peptides:...Ch. 3 - REFECT AND APPLY In each of the following two...Ch. 3 - REFECT AND APPLY Could the amino acid glycine...Ch. 3 - RECALL Sketch resonance structures for the peptide...Ch. 3 - RECALL How do the resonance structures of the...Ch. 3 - REFECT AND APPLY Would the peptide group be planar...Ch. 3 - Prob. 27RECh. 3 - REFECT AND APPLY Consider the peptides...Ch. 3 - REFECT AND APPLY Would you expect the titration...Ch. 3 - REFECT AND APPLY What are the sequences of all the...Ch. 3 - REFECT AND APPLY Answer Question 30 using...Ch. 3 - REFECT AND APPLY Most proteins contain more than...Ch. 3 - REFECT AND APPLY If the amino acids alanine and...Ch. 3 - Prob. 34RECh. 3 - REFECT AND APPLY Would the presence of a chiral...Ch. 3 - REFECT AND APPLY What might you infer (or know)...Ch. 3 - Prob. 37RECh. 3 - REFECT AND APPLY Suggest a reason why the amino...Ch. 3 - REFECT AND APPLY Consider the peptides...Ch. 3 - Prob. 40RECh. 3 - Prob. 41RECh. 3 - REFECT AND APPLY You are studying with a friend...Ch. 3 - Prob. 43RECh. 3 - REFECT AND APPLY Suggest a reason (or reasons) why...Ch. 3 - Prob. 45RECh. 3 - REFECT AND APPLY Speculate on the properties of...Ch. 3 - RECALL What are the structural differences between...Ch. 3 - RECALL How do the peptide hormones oxytocin and...Ch. 3 - RECALL What is the role of the disulfide bond in...Ch. 3 - RECALL Is it possible to form cyclic peptides...
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Match the three types of neurotransmitters to their relative size (largest to smallest): Largest Peptide neurotransmitter ✓ Second largest [Choose] Smallest > [Choose ] [Choose ] Amino acid neurotransmitter Peptide neurotransmitter Amine neurotransmitterarrow_forwardneed help not sure why its wrong please helparrow_forwardWhy the 2nd choice is correct?arrow_forward
- a) What are the differences between the Direct & Indirect Immunofluorescence Assays? (0.5 mark) b) What are the advantages of the Indirect Immunofluorescence Assays? (0.5 mark) c) A Super-Resolution Imaging Technique was developed in 2018 using imidazole, a His-tag ligand conjugated with a fluorophore to report the presence of a recombinant His-tag protein target, (Sci Rep, 2018, 8:5507). How does this technique improve the image quality? (2 marks)arrow_forwarda) What are the differences between the Direct & Indirect Immunofluorescence Assays? b) What are the advantages of the Indirect Immunofluorescence Assays? c) A Super-Resolution Imaging Technique was developed in 2018 using imidazole, a His-tag ligand conjugated with a fluorophore to report the presence of a recombinant His-tag protein target, (Sci Rep, 2018, 8:5507). How does this technique improve the image quality?arrow_forwardCalculate the number of ATP produced from oxidation of 1 molecule of glucosearrow_forward
- Example 1: 1. Suppose an enzyme (MW = 5,000 g/mole) has a concentration of 0.05 mg/L. If the kcat is 1 x 10 s, what is the theoretical maximum reaction velocity for the enzyme? A) 1050 µM/s. B) 100 µM/s. C) 150 μM/s. D) 105 μM/s.arrow_forwardIn 1956, E. P. Kennedy and S. B. Weiss published their study of membrane lipid phosphatidylcholine (lecithin) synthesis in rat liver. Their hypothesis was that phosphocholine joined with some cellular component to yield lecithin. In an earlier experiment, incubating 32 P-labeled phosphocholine at physiological temperature (37 °C) with broken cells from rat liver yielded labeled lecithin. This became their assay for the enzymes involved in lecithin synthesis. Determine the optimal pH for this enzyme and characterize the enzyme activity at different pH values. -O-P-O-CH2-CH₁₂-N(CH3)3 Phosphocholine H₂C-O-C-R HC-O-C-R2 + + + Cell fraction + ? HC-O-P-O-CH₁₂-CH₂-N(CH), O Phosphatidylcholine The researchers then centrifuged the broken cell preparation to separate the membranes from the soluble proteins. They tested three preparations: whole extract, membranes, and soluble proteins. Table 1 summarizes the results. Table 1: Cell fraction requirement for incorporation of 32p-phosphocholine into…arrow_forwardResearchers isolated an unknown substance, X, from rabbit muscle. They determined its structure from the following observations and experiments. (a) Qualitative analysis showed that X was composed entirely of C, H, and O. A weighed sample of X was completely oxidized and the H2O and CO2 produced were measured. This quantitative analysis revealed that X contained 40.00% C, 6.71% H, and 53.29% O by weight. (b) The molecular mass of X, as determined by mass spectrometry, was 90.00 atomic mass units (u). (c) Infrared spectroscopy showed that X contained one double bond. (d) X dissolved readily in water, and the solution demonstrated optical activity when tested in a polarimeter. (e) The aqueous solution of X is acidic. What is the empirical formula of X?arrow_forward
- Show work. don't give Ai generated solution....give correct solutionarrow_forwardBiochemistry What is the process of "transamination" in either the muscles or the liver, that involves keto acid or glutamic acid? Please explain how the steps work. Thank you!arrow_forwardBiochemistry Please help. Thank you What is the importance of glutamic acid in the metabolism of nitrogen from amino acids? (we know therole; it’s used to remove the nitrogen from amino acids so that the remaining carbon skeleton can bebroken down by the “usual” pathways, but what is the important, unique role that only glutamicacid/glutamate can do?)arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY