Textbook Question
Identify the amino acids and type of interaction that occurs between the following R groups in tertiary protein structures:
c. —CH2—SH and HS—CH2—
Ch.16 Amino Acids, Proteins, and Enzymes
Timberlake13th EditionChemistry: An Introduction to General, Organic, and Biological ChemistryISBN: 9780134421353
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Table of contents
- Ch.1 Chemistry in Our Lives11
- Ch.2 Chemistry and Measurements80
- Ch.3 Matter and Energy54
- Ch.4 Atoms and Elements51
- Ch.5 Nuclear Chemistry42
- Ch.6 Ionic and Molecular Compounds57
- Ch.7 Chemical Quantities and Reactions41
- Ch.8 Gases29
- Ch.9 Solutions51
- Ch.10 Acids and Bases and Equilibrium65
- Ch.11 Introduction to Organic Chemistry: Hydrocarbons78
- Ch.12 Alcohols, Thiols, Ethers, Aldehydes, and Ketones83
- Ch.13 Carbohydrates54
- Ch.14 Carboxylic Acids, Esters, Amines, and Amides90
- Ch.15 Lipids61
- Ch.16 Amino Acids, Proteins, and Enzymes84
- Ch.17 Nucleic Acids and Protein Synthesis83
- Ch.18 Metabolic Pathways and ATP Production67
Timberlake13th EditionChemistry: An Introduction to General, Organic, and Biological ChemistryISBN: 9780134421353Not the one you use?Change textbook
Chapter 16, Problem 59a
Identify the amino acids and type of interaction that occurs between the following R groups in tertiary protein structures:
a. 
Verified step by step guidance1
Examine the R groups of the amino acids in the provided image. Identify the functional groups present in each R group, such as hydroxyl (-OH), carboxyl (-COOH), amine (-NH2), or nonpolar hydrocarbon chains.
Determine the specific amino acids based on the structure of their R groups. For example, if the R group contains a hydroxyl group attached to a benzene ring, it is likely tyrosine.
Classify the type of interaction that can occur between the two R groups. Common interactions in tertiary protein structures include hydrogen bonding, ionic interactions, hydrophobic interactions, and disulfide bonds.
Match the identified amino acids to their respective interaction types. For example, if one R group has a carboxyl group and the other has an amine group, the interaction is likely ionic.
Summarize the findings by naming the amino acids and specifying the type of interaction that occurs between their R groups in the tertiary protein structure.
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Key Concepts
Here are the essential concepts you must grasp in order to answer the question correctly.
Amino Acids
Amino acids are the building blocks of proteins, consisting of a central carbon atom, an amino group, a carboxyl group, a hydrogen atom, and a variable R group (side chain). The properties of the R groups determine the characteristics of the amino acids, influencing how they interact with each other and fold into specific three-dimensional structures. Understanding the nature of these R groups is essential for analyzing protein interactions.
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Tertiary Structure
The tertiary structure of a protein refers to its overall three-dimensional shape, formed by the folding and interactions of its polypeptide chains. This structure is stabilized by various interactions among the R groups of amino acids, including hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges. The tertiary structure is crucial for the protein's functionality and biological activity.
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Types of Interactions
In tertiary protein structures, several types of interactions occur between R groups, including hydrophobic interactions, where nonpolar side chains cluster away from water; hydrogen bonds, which form between polar side chains; ionic bonds, which occur between positively and negatively charged side chains; and disulfide bridges, which are covalent bonds formed between cysteine residues. Recognizing these interactions is vital for understanding how proteins achieve their functional conformations.
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Related Practice
Textbook Question
Adults who are lactose intolerant cannot break down the disaccharide in milk products. To help digest dairy food, a product known as Lactaid can be added to milk and the milk then refrigerated for 24 hours.
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b. What might happen to the enzyme if the Lactaid were stored at 55 °C?
Textbook Question
What type of interaction would you expect between the following in a tertiary structure?
a. threonine and glutamine
Textbook Question
Draw the condensed structural formula for Ser–Lys–Asp.
Textbook Question
Fresh pineapple contains the enzyme bromelain that hydrolyzes peptide bonds in proteins.
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a. The directions for a gelatin (protein) dessert say not to add fresh pineapple. However, canned pineapple where pineapple is heated to high temperatures can be added. Why?
Textbook Question
Fresh pineapple contains the enzyme bromelain that hydrolyzes peptide bonds in proteins.
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b. Fresh pineapple is used in a marinade to tenderize tough meat. Why?