Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Question
Chapter 10, Problem 38P
Interpretation Introduction
Interpretation:
The fact that there is a lysine residue in the trypsin inhibitor that binds to the trypsin, but it is not a substrate needs to be explained.
Concept introduction:
The organic compounds that contain
A molecule that disturbs or inhibits the activity of an enzyme is known as enzyme inhibitor.
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Activity:
Write the line structure of each of the following peptide at pH7 and identify how many peptide bond in each
number.
1. Glycyl-valyl-serine
2. Threonyl-cysteine
3. Isoleucyl-methionyl-aspartate
Serine protease enzyme mutation
To show differences in the effect of the nucleophilic attack of the carbonyl group (C=O) of peptide bond between the catalytic triad of serine, histidine and aspartic acid, and another catalytic triad contains alanine, histidine and aspartic acid
Provide/ draw an example of catalytic mechanism with catalytic triad contains alanine, histidine and aspartic
Please answer completely will give rating surely
Modified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true.
Extreme temperatures and pH can cause permanent disruption of the protein primary structure(s) of enzymes that leads to loss of active site shape, loss of binding efficiency and activity.
Chapter 10 Solutions
Biochemistry
Ch. 10 - Prob. 1PCh. 10 - Prob. 2PCh. 10 - Prob. 3PCh. 10 - Prob. 4PCh. 10 - Prob. 5PCh. 10 - Prob. 6PCh. 10 - Prob. 7PCh. 10 - Prob. 8PCh. 10 - Prob. 9PCh. 10 - Prob. 10P
Ch. 10 - Prob. 11PCh. 10 - Prob. 12PCh. 10 - Prob. 13PCh. 10 - Prob. 14PCh. 10 - Prob. 15PCh. 10 - Prob. 16PCh. 10 - Prob. 17PCh. 10 - Prob. 18PCh. 10 - Prob. 19PCh. 10 - Prob. 20PCh. 10 - Prob. 21PCh. 10 - Prob. 22PCh. 10 - Prob. 23PCh. 10 - Prob. 24PCh. 10 - Prob. 25PCh. 10 - Prob. 26PCh. 10 - Prob. 27PCh. 10 - Prob. 28PCh. 10 - Prob. 29PCh. 10 - Prob. 30PCh. 10 - Prob. 31PCh. 10 - Prob. 32PCh. 10 - Prob. 33PCh. 10 - Prob. 34PCh. 10 - Prob. 35PCh. 10 - Prob. 36PCh. 10 - Prob. 37PCh. 10 - Prob. 38PCh. 10 - Prob. 39PCh. 10 - Prob. 40PCh. 10 - Prob. 41PCh. 10 - Prob. 42PCh. 10 - Prob. 43P
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- resting state of the protein, the Lys 216 Schiff base has pKa = 9.5 and Asp 85 has pKa = 3.5. When the conformational change occurs, the proton that was on the Schiff base moves to Asp 85. This should tell you that one or both of these two pKas changed with the conformational change. How does the pKa of Asp 85 compare with the pKa of the Lys 216 Schiff base after the conformational change?arrow_forwardReposting - What would the tertiary structure of the dipeptide Asp-Ser be if it was made into a polypeptide chain? (Would it form a beta pleated sheet, an alpha helix, etc) Why would it do this? What properties of this polypeptide causes this? This sub part still needs to be solved - What would the tertiary structure of Pro-ala and Glycl-L-alanine be?arrow_forwardWhy is the reaction rate low at pH7? Be specific and say something about the enzyme structure at the molecular level!arrow_forward
- Working at cross-purposes? Gluconeogenesis takes place during intense exercise, which seems counterintuitive. Why would an organism synthesize glucose and at the same time use glucose to generate energy?arrow_forwardBIOMOLECULES - MULTIPLE CHOICE - Please answer properly QUESTION : In human beings, what is the major control of de novo pyrimidine nucleotide synthesis? A. substrate availability B. competitive inhibition of carbamoyl phosphate synthetase II C. feedback inhibition of glutamine-PRPP amidotransferase D. vailability of N-acetyl glutamatearrow_forwardProtein folding with PDI and Peptidyl-prolyl isomerasearrow_forward
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