EBK LABORATORY MANUAL FOR GENERAL, ORGA
3rd Edition
ISBN: 9780100668324
Author: Timberlake
Publisher: YUZU
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Chapter 10, Problem 10.90AP
Summary Introduction
To explain:
The fact that why pepsin has a very high catalytic activity at
Introduction:
Each enzyme has its optimal
Chymotrypsin is a protein hydrolyzing enzyme found in small intestine that breaks down the protein components of diet. The optimal
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8. The following proteins represent a wide range of molecular weights and
isoelectric points. Mr is the molecular weight of a single protein chain.
• Protein 1: Mr 68,544; pl 6.11 (monomer)
• Protein 2: Mr 29,041; pl 5.32 (dimer)
• Protein 3: Mr 15,805; pl 5.7 (dimer)
• Protein 4: Mr 12,165; pl 4.74
a. Which protein is the most acidic? Explain your answer.
b. Which protein will migrate the slowest in an SDS-PAGE? Explain your
answer.
c. In what order will these proteins elute from a cation exchanger at pH 8?
Explain your answer.
d. In what order will these proteins salt out from a pH 7 solution by the
dropwise addition of saturated ammonium sulfate? Explain your answer.
5
83°F Cloudy
1. What are the solubility characteristics
globular proteins?
2. What kinds of important functions do
globular proteins have?
3. Explain why a protein such as casein pre-
cipitates from solution at its isoelectric
point.
A protein has a stability ranging from 6 to 15 kcal/mole at 37 OC. Stability is a measureof the equilibrium between the folded and unfolded protein given by the relationship;
folded(F) = unfolded (U), k=[U]/[F]
For a protein with a stability of 10 kcal/mole, calculate the fraction of unfolded proteinthat would exist at equilibrium at 37 OC. Use the following equation:GO=RTlnk=-2.3RTlog k,where R=1.98 x 10-3
kcal/mole and T is temperature in Kelvin (K) and k is theequilibrium constant.
Chapter 10 Solutions
EBK LABORATORY MANUAL FOR GENERAL, ORGA
Ch. 10 - Prob. 10.1PPCh. 10 - Classify each of the amino acids in Problem 10.1...Ch. 10 - Prob. 10.3PPCh. 10 - Prob. 10.4PPCh. 10 - Prob. 10.5PPCh. 10 - Give the three-letter and one-letter abbreviations...Ch. 10 - Prob. 10.7PPCh. 10 - Prob. 10.8PPCh. 10 - Prob. 10.10PPCh. 10 - Prob. 10.11PP
Ch. 10 - Consider the following tripeptide: a. Circle the...Ch. 10 - Consider the following tripeptide: a. Circle the...Ch. 10 - Prob. 10.15PPCh. 10 - Prob. 10.16PPCh. 10 - Prob. 10.17PPCh. 10 - Prob. 10.18PPCh. 10 - Prob. 10.19PPCh. 10 - How many different tripeptides that contain one...Ch. 10 - Prob. 10.21PPCh. 10 - When a protein folds into its tertiary .structure,...Ch. 10 - Prob. 10.23PPCh. 10 - What type of interaction would you expect between...Ch. 10 - Prob. 10.25PPCh. 10 - Determine whether each of the following statements...Ch. 10 - Determine whether each of the following statements...Ch. 10 - Prob. 10.28PPCh. 10 - Prob. 10.29PPCh. 10 - How do beta-amyloid plaques form in a person with...Ch. 10 - List the type of attractive force disrupted and...Ch. 10 - List the type of attractive force disrupted and...Ch. 10 - Identity each of the following statements as...Ch. 10 - Prob. 10.34PPCh. 10 - Prob. 10.35PPCh. 10 - Prob. 10.36PPCh. 10 - Prob. 10.37PPCh. 10 - Prob. 10.38PPCh. 10 - Prob. 10.39PPCh. 10 - Prob. 10.40PPCh. 10 - Prob. 10.41PPCh. 10 - Describe how a substrate is drawn to an enzyme to...Ch. 10 - Which model for enzyme-substrate interaction...Ch. 10 - Describe the key difference in the lock-and-key...Ch. 10 - Prob. 10.45PPCh. 10 - Prob. 10.46PPCh. 10 - How would the following changes affect enzyme...Ch. 10 - Chymotrypsin is an enzyme located in the small...Ch. 10 - Prob. 10.49PPCh. 10 - Indicate whether each of the following describes a...Ch. 10 - Prob. 10.51APCh. 10 - Give the name and three-letter abbreviation for...Ch. 10 - Give ihe name and three-letter abbreviation for...Ch. 10 - Prob. 10.54APCh. 10 - Prob. 10.55APCh. 10 - Aspartame, which is commonly known as Nutrasweet,...Ch. 10 - Prob. 10.57APCh. 10 - Prob. 10.58APCh. 10 - Consider the amino acids glycine, proline, and...Ch. 10 - a. Draw the structure of ValAlaLeu. b. Would you...Ch. 10 - a. Draw the structure of SerLysAsp. b. Would you...Ch. 10 - Name the covalent bond that helps to stabilize the...Ch. 10 - Prob. 10.63APCh. 10 - Prob. 10.64APCh. 10 - Prob. 10.65APCh. 10 - Identify the level of protein structure associated...Ch. 10 - Prob. 10.67APCh. 10 - Prob. 10.68APCh. 10 - Prob. 10.69APCh. 10 - Describe the changes that occur in the primary...Ch. 10 - What types of covalent bonds can be disrupted when...Ch. 10 - Prob. 10.72APCh. 10 - Prob. 10.73APCh. 10 - Prob. 10.74APCh. 10 - Prob. 10.75APCh. 10 - Prob. 10.76APCh. 10 - Prob. 10.77APCh. 10 - Match the terms (1) ES, (2) enzyme, and (3)...Ch. 10 - Match the terms (1) active site, (2) lock-and-key...Ch. 10 - Prob. 10.80APCh. 10 - The enzyme trypsin catalyzes the breakdown of many...Ch. 10 - Prob. 10.82APCh. 10 - Prob. 10.83APCh. 10 - What type of interactions between an enzyme and...Ch. 10 - Prob. 10.85APCh. 10 - Prob. 10.86APCh. 10 - Prob. 10.87APCh. 10 - Chymoirypsin, an enzyme that hydrolyzes peptide...Ch. 10 - Prob. 10.89APCh. 10 - Prob. 10.90APCh. 10 - Prob. 10.91APCh. 10 - Prob. 10.92APCh. 10 - Prob. 10.93APCh. 10 - When lead acts as a poison, it can do so by either...Ch. 10 - Increasing the substrate concentration of an...Ch. 10 - Prob. 10.96APCh. 10 - Prob. 10.97APCh. 10 - Meats spoil due to the action of enzymes that...Ch. 10 - Prob. 10.99APCh. 10 - Fresh pineapple contains the enzyme bromelain,...Ch. 10 - Prob. 10.101CPCh. 10 - Prob. 10.102CPCh. 10 - How is the structure of a soap micelle (Chapter 7)...Ch. 10 - Prob. 10.104CPCh. 10 - Prob. 10.105CPCh. 10 - Prob. 10.106CPCh. 10 - What is an essential amino acid?Ch. 10 - Prob. 1IA.2QCh. 10 - Prob. 1IA.3QCh. 10 - Prob. 1IA.4QCh. 10 - Locate the side chain (R) on each amino acid...Ch. 10 - Prob. 1IA.6QCh. 10 - Prob. 2IA.1QCh. 10 - In the preceding condensation reaction, a...Ch. 10 - Prob. 2IA.3QCh. 10 - Prob. 3IA.1QCh. 10 - Lactase, the enzyme that hydrolyzes the...Ch. 10 - Prob. 3IA.3QCh. 10 - Prob. 3IA.4QCh. 10 - Prob. 3IA.5QCh. 10 - Prob. 3IA.6QCh. 10 - Prob. 3IA.7QCh. 10 - Prob. 1ICCh. 10 - Find out how oxygen binding to hemoglobin changes...Ch. 10 - Prob. 3ICCh. 10 - Find out how penicillin acts as an antibiotic.
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- How is enzyme specificity explained by the lock-and-key theory?arrow_forwardThe isoelectric point, pl, of the protein trypsin is 10.5, while that of glyceraldehyde-3-phosphate dehydrogenase is 6.55. What is the net charge of trypsin at pH 5.1 ?[ What is the net charge of glyceraldehyde-3-phosphate dehydrogenase at pH 6.1 ?[ The isoelectric point of glutamic acid is 3.22; asparagine, 5.41. During paper electrophoresis at pH 6, toward which electrode does glutamic acid migrate? | During paper electrophoresis at pH 6.5, toward which electrode does asparagine migrate? [arrow_forward311. Which is the best binding pocket for phenylalanine? Ho H₂O Ho Ho 99 CH, CH₂ protein c. Ho H;o -CH₂ protein H,O b. H.0 protein HD d. H,0 Ho protein H₂Oarrow_forward
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