BIOCHEMISTRY (LOOSELEAF)-W/ACCESS
9th Edition
ISBN: 9781319425784
Author: BERG
Publisher: Macmillan Higher Education
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Chapter 9, Problem 14P
Interpretation Introduction
Interpretation:
The mechanism corresponding to the ATPase activity of the mutated enzyme is to be stated.
Concept introduction:
Enzymes being the catalysts increase the
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A Leu →Ala mutation at a site buried in the core of the enzyme lysozymeis found to be destabilizing. Explain the observed effect of this mutationon lysozyme stability by predicting how enthalpy (ΔH°), conformationalentropy (ΔS°peptide), and the hydrophobic effect (ΔS°solvent) are expected to change for the mutant compared to wild-type lysozyme. Explain how ΔG°for unfolding is affected by your predicted changes in enthalpy or entropy.
10-¹1 M. A 1 nM (10-⁹ M) solution of lysozyme is
o An Fab fragment binds to lysozyme with a dissociation constant of Kå
treated with increasing concentrations of the Fab fragment. At what concentration of added Fab will half of the lysozyme be
bound to the Fab?
[F] =
nM
Hi - I have the following as a question in my biochemistry course and I am just lost on where to start. Thanks!
Cyt cb562 will form a tetramer in the presence of Zn+2 or in the absence of Zn+2, it will form a trimer. For both the tetramer and the trimer, suggest the identity of three different amino acids that could be on the interface. Explain how your selections facilitate these interactions.
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