Biochemistry 410/411 Textbook - 5th Edition - Custom Texas A&M University
5th Edition
ISBN: 9781119302940
Author: Voet
Publisher: WILEY C
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Chapter 11, Problem 14E
Summary Introduction
To explain: The reason behind Person W who stated that it is meaningless to distinguish between the binding sites and catalytic sites.
Concept introduction: Enzymes are the biocatalyst that accelerate the
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Chapter 11 Solutions
Biochemistry 410/411 Textbook - 5th Edition - Custom Texas A&M University
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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- Fura-2 Fluorescence (Arbitrary Unit) 4500 4000 3500 3000 2500 2000 1500 1000 500 [Ca2+]=2970nM, 25°C [Ca2+] 2970nM, 4°C [Ca2+]=0.9nM, 25°C [Ca2+] = 0.9nM, 4°C 0 260 280 300 340 360 380 400 420 440 Wavelength (nm) ← < The figure on the LHS shows the excitation spectra of Fura-2 (Em = 510 nm) in 2 solutions with two different Ca2+ ion concentration as indicated. Except for temperature, the setting for excitation & signal acquisition was identical.< ப a) The unit in Y-axis is arbitrary (unspecified). Why? < < b) Compare & contrast the excitation wavelength of the Isosbestic Point of Fura-2 at 25 °C & 4 °C. Give a possible reason for the discrepancy. < c) The fluorescence intensity at 25 °C & 4 °C are different. Explain why with the concept of electronic configuration. <arrow_forwarddraw in the structure of each amino acid (as L-amino acids) using the Fischer projection style. an example has been included. Draw the structure for glycine, alanine, valine, isoleucine, methionine, proline, phenylalanine, tryptophan, serine, threonine, asparagine, glutamine, lysine, arginine, aspartic acid, glutamic acid, histidine, tyrosine, cysteinearrow_forwarddraw in the structure of each amino acid (as L-amino acids) using the Fischer projection style. an example has been includedarrow_forward
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