1. a. Draw the following pentapeptide:lysine-leucine-aspartate-threonine-phenylalanineb. Label the amino and carboxyl terminus of your peptidec. Label each amino acid residue with one and three letter abbreviationsd. Label the alpha carbonse. Label the bonds around which phi and psi rotational angles occurf. Which amino acid in this chain is most likely to be phosphorylated? Which amino acid is mostlikely to be acetylated?

In the drawn pentapeptide, each amino acid is represented by a letter code, and the peptide bond is…

Answered: 1. a. Draw the following pentapeptide:…

Concepts of Biology

1st Edition

ISBN:9781938168116

Author:Samantha Fowler, Rebecca Roush, James Wise

Publisher:Samantha Fowler, Rebecca Roush, James Wise

Chapter2: Chemistry Of Life

Section: Chapter Questions

Problem 16CTQ: Explain what happens if even one amino acid is substituted for another in a polypeptide chain....

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Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.
Polypeptide folding is often mediated by other proteins called chaperones. Describe how a mutant chaperone protein might be responsible for a genetic disorder involving an enzyme.
Explain what happens if even one amino acid is substituted for another in a polypeptide chain. Provide a specific example.
Figure 3.5 What kind of sugars are these, aldose or ketose?
The synthetic process by which monomers are covalently linked is (a) hydrolysis (b) isomerization (c) condensation (d) glycosidic linkage (e) ester linkage
Lactose is a disaccharide formed by the formation of a bond between glucose and glycosidic; lactose glycosidic; galactose hydrogen; sucrose hydrogen; fructose
Uracil ________. contains nitrogen is a pyrimidine is found in RNA all of the above
Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.
a. Can a mutation change a proteins tertiary structure without changing its primary structure? b. Can a mutation change a proteins primary structure without affecting its secondary structure?
Figure 16.13 An increase in phosphorylation levels of elF-2 has been observed in patients with neurodegenerative diseases such as Alzheimer’s, Parkinson's, and Huntington's. What impact do you think this might have on protein synthesis?
Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternary

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