Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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- 3. Which best describes the contribution of tertiary (3’) structure of to the native conformation of polypeptides and proteins: a) Structure that results from intrachain interactions of amino acid side chains b) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence of amino acids from beginning to end of moleculearrow_forward4. Explain and draw a representative picture of the four levels of protein structure. How are they defined and what bonds keep them together? ? What effect does the aarrow_forward1. Is there more than one way to fold a protein, given the conflicting demands of the different "R" groups and the protein existing in a watery environment? 2. Explain what an R group is. 3. Compare the backbone of a polypeptide with that of a nucleic acid. 4. Proteins perform critical functions in all of our cells. Without proteins, life wouldn’t exist. Think of some specific proteins and describe what function they perform. 5. Explain the difference between secondary and tertiary protein structures.arrow_forward
- 4. A protein solution is prepared by dissolving 350 µg of protein in 200 µL of water. A 150 μL sample of this solution is diluted to a total volume of 4.5 mL. How many mg of protein will be in a 2 mL sample of the diluted protein solution? Space to show your workings:arrow_forward42.arrow_forward4.) If a mutation in an organisms DNA causes the resulting protein to possess an alanine residue to be in the 13th position instead of a glycine, what level(s) of the resulting protein's structure would likely be affected? Why? Why would the other(s) not be affected? 14:arrow_forward
- 32. Would you expect to find hydrophobic amino acids on the external surface or internally in proteins? Why?arrow_forward3. A biochemist purified a protein from the bloodstream and determined its molecular weight under several conditions. In 8 M urea, which denatures the polypeptide chain, the molecular weight of the protein was 150,000 Da. She found that under reducing conditions the molecular weight of the protein was 75,000 Da, while under oxidizing conditions the molecular weight of the protein was 150,000 Da. Explain these results.arrow_forward4. What type of tertiary structure interactions are most likely between the following amino acids? (Use a reference chart as necessary.) (b) methionine and methionine (a) glycine and valine (d) serine and lysine (c) cysteine and cysteinearrow_forward
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