Biochemistry: Concepts and Connections (2nd Edition)
Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
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 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
Peptides     and     small     proteins     fold     spontaneously     in     aqueous     solution     at     room    temperature.     Thus,     for     a     small     protein     in     water,     we     can     say ΔG FOLD < 0.          Denoting     the    unfolded    protein    as    Unf and    the    folded    protein    as    Fld,    we    can    write    the    following    equation:Unf(aq)--DELTA G FOLD----> Fld(aq)Considering    the    transition    from    the    unfolded    state    (in    which    there    are    many    possible    conformations)    to    the    folded    state    (only    one    conformation),    there    is    clearly    a    decrease in    the    entropy    of    the    protein.    However,    protein    folding    is    (correctly)    described    as    an    entropically    driven    process.a) Resolve    this    apparent    paradox    by    identifying    the    enthalpy (ΔH)    and    entropy (−TΔS)components    involved    in    protein…
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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