Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Chapter 2, Problem 12P
Interpretation Introduction
Interpretation:
The meaning of the term polypeptide backbone should be determined.
Concept introduction:
A peptide bond exists between the two amino acids. During the formation of a peptide bond, a molecule of water is released. The carboxyl group of one amino acid gets linked with the amino group of the other amino acid. Polypeptides and proteins are the chains formed by the amino acids.
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Which one of these is correct ? And why are the rest incorrect?
Suppose that there is a protein consisting of two polypeptide chains with the given sequences in the picture.
What will be the expected result if a biochemist does an end-group analysis to identify the N and C terminal residues of the protein? Explain why.
Figure 7 shows one additional type of bond that can stabilize the tertiary structure of a
protein. This bond is called a disulfide bond (or disulfide bridge), and it involves the
sulfhydryl (-SH) R groups from one particular type of amino acid. A disulfide bond can
form only under certain conditions (oxidative conditions). We'll talk about oxidation and
reduction next week. For now, just note that this type of bond does exist in some
proteins.
Answer the below questions on tertiary structure in your own document.
8. Figure 6 shows examples of bonds that might stabilize the tertiary structure of a
protein (labeled A, B, and C). Do these interactions involve only the amino acid R
groups, only the polypeptide backbone atoms, or both?
9. In the table below, indicate what type of bond/ interaction is represented in
the examples shown in Figure 6, panels A, B, and C and whether each
interaction involves group or backbone atoms.
Example
Type of Bonding Interaction
R group or backbone?
A
В
10.…
Chapter 2 Solutions
Biochemistry
Ch. 2 - Prob. 1PCh. 2 - Prob. 2PCh. 2 - Prob. 3PCh. 2 - Prob. 4PCh. 2 - Prob. 5PCh. 2 - Prob. 6PCh. 2 - Prob. 7PCh. 2 - Prob. 8PCh. 2 - Prob. 9PCh. 2 - Prob. 10P
Ch. 2 - Prob. 11PCh. 2 - Prob. 12PCh. 2 - Prob. 13PCh. 2 - Prob. 14PCh. 2 - Prob. 15PCh. 2 - Prob. 16PCh. 2 - Prob. 17PCh. 2 - Prob. 18PCh. 2 - Prob. 19PCh. 2 - Prob. 20PCh. 2 - Prob. 21PCh. 2 - Prob. 22PCh. 2 - Prob. 23PCh. 2 - Prob. 24PCh. 2 - Prob. 25PCh. 2 - Prob. 26PCh. 2 - Prob. 27PCh. 2 - Prob. 28PCh. 2 - Prob. 29PCh. 2 - Prob. 30PCh. 2 - Prob. 31PCh. 2 - Prob. 32PCh. 2 - Prob. 33PCh. 2 - Prob. 34PCh. 2 - Prob. 35PCh. 2 - Prob. 36PCh. 2 - Prob. 37P
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- Part I. Protein structure You have the toy model for a protein in the water (W) environment of the cell shown. a) How many residues (amino acids) does this toy protein have? b) How many hydrophobic (H), hydrophilic (P), and charged (C) residues are there? c) Sketch the molecule on your answer sheet and then show the positions of the favorable C-C (charge-charge) interactions on the figure.arrow_forwardPlz do Asap...! Plz provide proper explanation ....!arrow_forwardMacmillan Learning The graphs show a titration curve for the amino acid histidine. Label the fist curve with the major histidine species at each position. One histidine species will not be used. Label the second curve with the pKå values for the histidine functional groups and the isoelectric point (pI) of histidine. 14 12 10 pH 6 8 4 His²+ 2 His+ 0 0.0 0.5 1.0 Incorrect Answer His²- [His²+] = [His*] 1.5 [OH-] (equivalents) Hisº His [His]=[His] 2.0 2.5 3.0 Answer Bank [His+] = [His]arrow_forward
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