Biological Science (6th Edition)
6th Edition
ISBN: 9780321976499
Author: Scott Freeman, Kim Quillin, Lizabeth Allison, Michael Black, Emily Taylor, Greg Podgorski, Jeff Carmichael
Publisher: PEARSON
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Textbook Question
Chapter 3, Problem 14PIAT
Recall that proline often introduces kinks in the backbone of a polypeptide. These kinks make it difficult for enzymes in your gut to fully digest gluten. In people with celiac disease, certain proline-rich peptides left over after gluten digestion will trigger an abnormal immune response. Researchers have identified a mold enzyme called AN-PEP that effectively digests proline-rich peptides. Predict where the structural differences would occur between AN-PEP and other enzymes that do not digest the peptides.
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A peptide with the primary structure Lys-Arg-Pro-Leu-Ile-Asp-Gly-Ala must be synthesized by the methods developed
by Merrifield.
Calculate the percentage of the peptides synthesized that will
be full length and have the correct sequence if the addition of
each amino acid residue is 96% efficient.
Do the calculation a second time but assume a 99% efficiency
for each cycle.
full-length peptides with the
correct sequence if 96% efficient:
full-length peptides with the
correct sequence if 99% efficient:
%
%
Consider the hypothetical serine protease in the image, which shows the specificity pockets. The S1 pocket is small and hydrophobic, the S2
pocket is deep and hydrophobic, and the S1' pocket has an aspartate residue in the bottom. If the amino acids involved are K, W, and G,
which pair is joined by the peptide bond that will be cleaved by the protease? MAKE SURE YOUR CHOICE REFLECTS THE S1-S ORDER
DESCRIBED.
S1
Rs
R1
Ri
H.
S2
S
OGK
OKAN
OwG
IZ
IZ
Many blood clotting proteins undergo a post-translational modification in which specific glutamic acid residues (Glu) in the protein are converted to gamma-carboxyglutamic acid residues (Gla). See reaction scheme below. An example is the blood clotting protein Factor IX, which has 12 Glu in its N-terminus converted to Gla. This modification gives Factor IX the ability to bind calcium and phospholipid membranes. Bacteria do not have the enzyme required to convert Glu to Gla and therefore Factor IX proteins expressed in bacteria would not have the proper modifications. How might you engineer the translational apparatus of a bacterial cell line so that it produces Factor IX with Gla in the appropriate positions. How would you ensure that only the 12 Glu in Factor IX that are normally converted to Gla and not just all Glu (Limit 5-6 senetnces)?
Chapter 3 Solutions
Biological Science (6th Edition)
Ch. 3 - 1. What two functional groups are bound to the...Ch. 3 - 2. What type of bond is directly involved in the...Ch. 3 - What type of information is used to direct...Ch. 3 - 4. What is an active site?
a. the location in an...Ch. 3 - Prob. 5TYUCh. 3 - Prob. 6TYUCh. 3 - 7. Why are proteins not considered to be a good...Ch. 3 - Prob. 8TYUCh. 3 - Prob. 9TYPSSCh. 3 - 10. Make a concept map (see BioSkills 12) that...
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