3. One of the 20 standard amino acids is unusual in that its side chain contains a ring that incorporates the amine functional group of the amino acid. What is the name of this amino acid? What is its three-letter abbreviation and one-letter code? Write the chemical structure of this amino acid at physiological pH.

3. One of the 20 standard amino acids is unusual in that its side chain contains a ring that incorporates the amine functional group of the amino acid. What is the name of this amino acid? What is its three-letter abbreviation and one-letter code? Write the chemical structure of this amino acid at physiological pH.

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter3: Biological Molecules: The Carbon Compounds Of Life

Section: Chapter Questions

Problem 8TYK: The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices...

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The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices unwind. c. sheet structures unfold. d. tertiary structure is changed. e. quaternary structures disassemble.
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1. Which of the following forms of lysine would you expect to predominate at low pH, neutral pH and high pH? 2. One of the 20 amino acids is unusual in that its side chain contains a ring that incorporates the amine functional group of the amino acid. What is the name of this amino acid? Write the chemical structure of this amino acid at physiological pH.
1.Describe in detail how to detect the primary structure of protein. 2.Given a mixture of lysine,histidine and cysteine.The isoelectronic point of the amino acids are as follows: histidine:7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.
3. How many amino acids are there in the polypeptide (protein)?
1.Describe in detail how to determine the primary structure of protein. 2.You have been given a mixture of lysine, histidine and cysteine.The isoelectric point of the amino acids are as follows; histidine 7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.
1. What is an amino acid that has aromatic heterocyclic side chain?
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1.What reactive groups are involved in the formation of a peptide bond?2.A molecule of what substance must be removed in order to form a peptide bond?
6. Which amino acid would most likely be found on the surface of a protein molecule at physiological pH? a. Isoleucine b. Lysine c. Alanine d. Proline 7. Which of the following statements about terpenes is NOT true? a. They are a type of terpenoid. b. They all contain double bonds. c. They are all made up of 5-carbon units. d. They all contain oxygen. 8. How are the plasma membranes of mammalian and bacterial cells similar? a. They typically contain cholesterol. b. They have negatively charged lipids on their surfaces. c. They contain lipids that are involved in signal transduction. d. They are made up of many different types of phospholipids.
2- ‏Some proteins contain additional amino acids that arise by modification of an amino acid already present in a peptide , examples include: a) Gamma Amino Butyric Acid. b) 5 - hydroxy Lysine c) 4 - hydroxy proline d) All of the above e) None of the above
1)Explain 3 benefits of proteins forming higher oligomeric states. 2) Why are peptide bonds planar?