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Concept explainers
Cartoon renderings of the proteins Top 7 and adaH2 are shown below. Both are soluble, densely packed proteins of roughly 96 residues, and each has a topology of 2 a helices packed onto a 5-stranded ß sheet.
The accompanying table lists some information about the amino acid composition and values of ΔS0 for the folding of these proteins (i.e. for Unfolded →Folded) at 250C. Based on the information in the table, which protein do you predict buries the greater hydrophobic surface area upon folding? Assume 2-state folding (i.e., no intermediates), and that the Unfolded state for both proteins is 100% solvent-exposed. Explain your answer in terms of expected contributions from ΔS0peptide and ΔS0solvent.
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Chapter 6 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
- Show a mechanism that leads to the opening of the ring below under acid-catalyzed conditions. Give the correct Fischer projection for this sugar.arrow_forwardWhat is the stereochemical relationship between B & C?arrow_forwardDon't use ai or any chat gpt will dislike okk just use accurate information okkk okkk just solve full accurate. don't use guidelines okk just did it accurate 100% sure experts solve it correct complete solutions okkk follow all instructions requirements okkkarrow_forward
- Problem 15 of 15 Submit Using the following reaction data points, construct Lineweaver-Burk plots for an enzyme with and without an inhibitor by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. Using the information from this plot, determine the type of inhibitor present. 1 mM-1 1 s mM -1 [S]' V' with 10 μg per 20 54 10 36 20 5 27 2.5 23 1.25 20 Answer: |||arrow_forward12:33 CO Problem 4 of 15 4G 54% Done On the following Lineweaver-Burk -1 plot, identify the by dragging the Km point to the appropriate value. 1/V 40 35- 30- 25 20 15 10- T Км -15 10 -5 0 5 ||| 10 15 №20 25 25 30 1/[S] Г powered by desmosarrow_forward1:30 5G 47% Problem 10 of 15 Submit Using the following reaction data points, construct a Lineweaver-Burk plot for an enzyme with and without a competitive inhibitor by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. 1 -1 1 mM [S]' s mM¹ with 10 mg pe 20 V' 54 10 36 > ст 5 27 2.5 23 1.25 20 Answer: |||arrow_forward
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