Pearson eText for Biochemistry: Concepts and Connections -- Instant Access (Pearson+)
Pearson eText for Biochemistry: Concepts and Connections -- Instant Access (Pearson+)
2nd Edition
ISBN: 9780137533114
Author: Dean Appling, Spencer Anthony-Cahill
Publisher: PEARSON+
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Chapter 6, Problem 7P

a. Based on a more conservative answer to Problem 6 (2.7 x 1092 conformations), estimate the conformational entropy change on folding a mole of this protein into a native structure with only one conformation. (Hint Consider Equation )
b. If the protein folds entirely into a helix with H bonds as the only source of enthalpy of stabilization, and each mole of H bonds contributes -5 kJ/mol to the enthalpy, estimate Δ Hfolding . Note that the ends of helices contain fewer hydrogen bonds per residue than in the middle (see Figure 6.4).
c. From your answers (a) and (b), estimate Δ Gfolding for this protem at 25oC. Is the folded form of the protein stable at 25oC?

6. Consider a small protein containing 101 amino acid residues. The protein backbone win have 200 bonds about which rotation can occur. Assume that three orientations are possible about each these bonds.
a. Based on these assumptions, about how many random-con conformations will be possible for this protein?
b. The estimate obtained in (a) is surety too large. Give one reason why.

Chapter 6, Problem 7P, a. Based on a more conservative answer to Problem 6 (2.7 x 1092 conformations), estimate the , example  1Chapter 6, Problem 7P, a. Based on a more conservative answer to Problem 6 (2.7 x 1092 conformations), estimate the , example  2Chapter 6, Problem 7P, a. Based on a more conservative answer to Problem 6 (2.7 x 1092 conformations), estimate the , example  3

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Protein concentration can readily be determined using the Beer-Lambert law: A = e l c where A = absorbance e = molar absorption coefficient (M-1cm-1) l = light path length (cm) c = concentration (M) If the molar absorption coefficient at 280 nm for yeast ADH is 48860 M-1cm-1 and a 10 mL solution of the protein has an absorbance at 280 nm of 0.4 (as measured by a spectrometer with pathlength 1 cm), then what is the concentration of the protein solution (in μM)? i.e. concentration = ______ μM   If the molecular weight of the protein is 36849, what is its concentration in mg/mL? i.e. concentration = _______ mg/mL For each part of the question, show your calculations to arrive at your answers.
The extinction coefficient or absorptivity (ɛ) of protein A at 340 nm is 6440 M-1 cm-1, whereas protein B does not absorb at 340 nm. What absorbance will be observed when light at 340 nm passes through a 5 mm cuvette containing 10 µM of protein A and 10 µM of protein B? Beer-Lambert-law; A = ɛ x C x1; A = absorbance, C= concentration, 1= pathlength).
The dissociation constant, Kd for a complex between protein A and protein B is 4.1 μM. If the two proteins are mixed together at initial concentrations of [A]= 0.025 μM and [B] = 4.7 μM, calculate (a) the equilibrium concentrations of A, B, and AB (the dimer formed by A and B) (b) the percentage of A bound to B
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Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY