Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Chapter 10, Problem 20P
The transport of aspirin (pKa = 3.5, structure shown here) form the digestive tract to the circulation occurs by nonmediated absorption into cells lining the stomach (where pH=0.8) and the small intestine (where pH=6.0). Do you expect absorption to be faster in the stomach or in the small intestine?
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Using the data in the table below, calculate the average molar mass of an amino acid residue in each of the proteins in the table (excluding cytochrome c, myoglobin, and hemoglobin). Next, calculate the mean of the mean molar mass considering all proteins (excluding cytochrome c, myoglobin and hemoglobin)
The transport of aspirin (pKa = 3.5, structure shown here) from the digestive tract to the circulation occurs by nonmediated absorption into cells lining the stomach (where pH = 0.8) and the small intestine (where pH 6.0). Do you expect absorption to be faster in the stomach or in the small intestine?
Chapter 10 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 10 - Prob. 1PCh. 10 - Given these molecular components--glycerol, fatty...Ch. 10 - The classic demonstration that cell plasma...Ch. 10 - The lipid portion of a typical bilayers is about...Ch. 10 - In the following situations, what is the free...Ch. 10 - Propose an experiment that would distinguish...Ch. 10 - Prob. 7PCh. 10 - Peptide hormones (such as insulin) must bind to...Ch. 10 - Prob. 9PCh. 10 - Prob. 10P
Ch. 10 - Prob. 11PCh. 10 - Prob. 12PCh. 10 - Prob. 13PCh. 10 - Prob. 14PCh. 10 - The concentration of glucose in your circulatory...Ch. 10 - ATP is synthesized from ADP, Pi , and a proton on...Ch. 10 - The Na+/ glucose symport transports glucose from...Ch. 10 - Prob. 18PCh. 10 - Prob. 19PCh. 10 - The transport of aspirin (pKa = 3.5, structure...Ch. 10 - Prob. 21P
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- Given the free amino acid Asparagine, at which pH would you expect to have equal numbers of positive and negative charges on the free Asparagine molecules in solution?arrow_forwardMany plasma proteins found in an aqueous environment are globular in shape. Which amino acid side chains would you expect to find on the surface of a globular protein and in contact with the aqueous environment? Which would you expect to find inside, shielded from the aqueous environment? Explain. Q.) Argarrow_forwardIs a protein as good a cellular buffer at physiological pH as its constituent amino acids would be if they were present as free amino acids in proportional concentrations in the cell? Explain Based on your rationale in the previous question, describe the difference in the dissociation constants of the α-COOH of GABA and glutamate, and the differences in the dissociation constants of the amino group in each of these amino acids.arrow_forward
- Using the data in the table below, calculate the average molar mass of an amino acid residue in each of the proteins in the table (excluding cytochrome c, myoglobin, and hemoglobin). Next, calculate the average molar mass considering all proteins (excluding cytochrome c, myoglobin and hemoglobin).arrow_forwardMany plasma proteins found in an aqueous environment are globular in shape. Which amino acid side chains would you expect to find on the surface of a globular protein and in contact with the aqueous environment? Which would you expect to find inside, shielded from the aqueous environment? Explain. Q.) Serarrow_forwardYou are given a pure protein sample to characterize and provided the following information: Its molar extinction coefficient, ε280, is 0.25 liters micromole-1 cm-1 in both the folded and unfolded form Its ΔGo for unfolding is 1.5 kcal/mol at 37o (where RT = 0.59 kcal/mole) A) Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 20-fold dilution of your pure protein in solution (by this, we mean that 50 ul of the protein sample was diluted to a final volume of 1 ml) and find A280 = 0.40. What is the original concentration of the protein before dilution? B) What is the concentration of the unfolded form of the protein in your sample?arrow_forward
- A hypothetical protein has a molar mass of 23,300 Da. Assume that the average molar mass of an amino acid is 120. • How many amino acids are present in this hypothetical protein? • What is the minimum number of codons present in the mRNA that codes for this protein? • What is the minimum number of nucleotides needed to code for this protein?arrow_forwardGiven the Ramachandran Plot below, identify the protein components that could adopt the phi-psi angle combination indicated by the number 3.arrow_forwardA 0.0284 M aqueous solution of lactic acid, HC3H5O3, a substance that accumulates in the blood and muscles during physical activity, is found to be 6.7% ionized. Determine the value of Ka for lactic acid.arrow_forward
- Currently, aspartic acid is forming an ionic interaction with arginine in a protein. Part a) If arginine is replaced with glutamic acid, would the ionic interaction have its stability increased, decreased, or have no effect on the ionic interaction? Part b) If arginine is replaced with Lysine, would the ionic interaction have its stability increased, decreased, or have no effect on the ionic interaction? Part c) If arginine is replaced with isoleucine, would the ionic interaction have its stability increased, decreased, or have no effect on the ionic interaction?arrow_forwarda) At what pH will you try to bind lysozyme to a cation exchanger? b) Is it possible to perform this binding even at a different pH than the one you mentioned in section a? Explain your answer. c) Is it possible to bind lysozyme to an anion exchanger as well? If so, at what pH?arrow_forwardOf the 20 protein-derived amino acids shown in Table 27.1, which contain Q.) no chiral centerarrow_forward
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