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 3, Problem 15P

The major difference between a protein molecule in its native state and in its denatured state lies in the number of conformations available. To a first approximation, the native, folded state can be thought to have one conformation. The unfolded state can be estimated to have three possible orientations about each bond between residues.
a. For a protein of 100 residues, estimate the entropy change per mole upon denaturation.
b. What must be the enthalpy change accompanying denaturation to allow the protein to be half-denatured at
50o C?
c. WiII the fraction denatured increase or decrease with increasing temperature?

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a) What are the differences between the Direct & Indirect Immunofluorescence Assays? (0.5 mark) b) What are the advantages of the Indirect Immunofluorescence Assays? (0.5 mark) c) A Super-Resolution Imaging Technique was developed in 2018 using imidazole, a His-tag ligand conjugated with a fluorophore to report the presence of a recombinant His-tag protein target, (Sci Rep, 2018, 8:5507). How does this technique improve the image quality? (2 marks)
a) What are the differences between the Direct & Indirect Immunofluorescence Assays?  b) What are the advantages of the Indirect Immunofluorescence Assays?  c) A Super-Resolution Imaging Technique was developed in 2018 using imidazole, a His-tag ligand conjugated with a fluorophore to report the presence of a recombinant His-tag protein target, (Sci Rep, 2018, 8:5507). How does this technique improve the image quality?
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