Fundamentals of Biochemistry: Life at the Molecular Level
5th Edition
ISBN: 9781118918401
Author: Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher: WILEY
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Chapter 11, Problem 29CQ
Summary Introduction
To explain: The reason behind the preparation of tofu that removes the trypsin inhibitor present in soybeans.
Concept introduction: Tofu is also known as bean curd that coagulates soymilk. It is an important source of dietary protein that provides all essential amino acids that are required from the diet. Trypsin is a pancreatic serine protease enzyme that involved in the digestion of food proteins and other biological process.
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Please help with this Mass Spectrometry Question. Thank you
For the mass spec. shown in the attached image, please determine and give the amino acid sequence of the pentapeptide. Show which end is the amino terminus and which is the carboxy terminus. How does one arrive at the solution?
Draw a tripeptide of your choosing at pH 7. Have the N-terminus on the left and the C-terminus on the right. Then:
Draw a triangle around the α-carbons.
Draw a box around the R-groups.
Circle the atoms capable of hydrogen bonding.
Highlight the atoms involved in the formation of the peptide bonds.
What type of structure have you drawn? (primary, secondary, tertiary or quaternary protein structure).
2. For the flow of fluid over a flat membrane of length 10cm,
determine the length-average mass transfer coefficient. The
relevant properties of the system are u=0.01cm²/s, D=5 x 106
cm²/s, and v = 5.0 cm/s.
Chapter 11 Solutions
Fundamentals of Biochemistry: Life at the Molecular Level
Ch. 11 - Prob. 1ECh. 11 - 2. What is the relationship between the rate of an...Ch. 11 - 3. Which type of enzyme (Table 11-2) catalyzes the...Ch. 11 - 4. Which type of enzyme (Table 11-2) catalyzes the...Ch. 11 - 5. On the free energy diagram shown, label the...Ch. 11 - Prob. 6ECh. 11 - 7. Approximately how much does staphylococcal...Ch. 11 - 8. Calculate the rate enhancement that could be...Ch. 11 - 9. Explain why enzyme activity varies with...Ch. 11 - 10. The covalent catalytic mechanism of an enzyme...
Ch. 11 - Prob. 11ECh. 11 - 12. Explain why RNase A cannot catalyze the...Ch. 11 - 13. Urease, the first enzyme to be crystallized,...Ch. 11 - 14. Wolfenden has stated that it is meaningless to...Ch. 11 - 15. Explain why lysozyme cleaves the artificial...Ch. 11 - 16. Would you expect lysozyme to hydrolyze...Ch. 11 - 17. Design a chloromethylketone inhibitor of...Ch. 11 - 18. Predict the effect of mutating Asp 102 of...Ch. 11 - 19. Diagram the hydrogen-bonding interactions of...Ch. 11 - Prob. 20ECh. 11 - 21. Using the reaction shown in Box 11-1 (the...Ch. 11 - Prob. 22CQCh. 11 - 23. What feature of RNA would allow it to function...Ch. 11 - 24. Suggest a transition state analog for proline...Ch. 11 - 25. Lysozyme residues Asp 101 and Arg 114 are...Ch. 11 - 26. Predict the effect on lysozyme’s activity of...Ch. 11 - Prob. 27CQCh. 11 - Prob. 28CQCh. 11 - Prob. 29CQCh. 11 - 30. Many of the cell’s hydrolytic enzymes are...Ch. 11 - Prob. 31CQCh. 11 - Prob. 32CQCh. 11 - Prob. 1MTE
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