Textbook Question
What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?
b. leucine and isoleucine
Ch.10 Proteins Workers of the Cell
Frost4th EditionGeneral, Organic and Biological ChemistryISBN: 9780134988696
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Table of contents
- Ch.4 Introduction to Organic Compounds75
- Ch.5 Chemical Reactions19
- Ch.6 Carbohydrates Life's Sweet Molecules62
- Ch.7 States of Matter and Their Attractive Forces8
- Ch.8 Solution Chemistry Sugar and Water Do Mix4
- Ch.10 Proteins Workers of the Cell89
- Ch.11 Nucleic Acids Big Molecules with a Big Role69
- Ch.12 Food as Fuel An Overview of Metabolism65
Frost4th EditionGeneral, Organic and Biological ChemistryISBN: 9780134988696Not the one you use?Change textbook
Chapter 6, Problem 27a
What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?
a. lysine and glutamate
Verified step by step guidance1
Identify the side chains of the given amino acids: Lysine has a positively charged amino group (-NH3+) in its side chain, while Glutamate has a negatively charged carboxylate group (-COO-) in its side chain.
Recall that opposite charges attract each other. This type of interaction is known as an ionic bond or salt bridge in the context of protein tertiary structure.
Determine the conditions under which this interaction is most likely to occur. Ionic bonds between side chains are strongest in environments where the pH allows the amino acid side chains to maintain their charges (e.g., lysine remains positively charged and glutamate remains negatively charged).
Understand the role of this interaction in protein structure. Ionic bonds contribute to the stabilization of the protein's tertiary structure by forming strong, specific attractions between oppositely charged side chains.
Conclude that the interaction between lysine and glutamate in the tertiary structure of a protein is an ionic bond (salt bridge) due to the attraction between their oppositely charged side chains.
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Key Concepts
Here are the essential concepts you must grasp in order to answer the question correctly.
Amino Acid Side Chains
Amino acids have unique side chains (R groups) that determine their chemical properties and interactions. These side chains can be polar, nonpolar, acidic, or basic, influencing how amino acids interact with each other in a protein's tertiary structure. Understanding the nature of these side chains is crucial for predicting interactions between specific amino acids.
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Intro to Amino Acids Concept 1
Ionic Interactions
Ionic interactions occur between positively and negatively charged side chains of amino acids. In the case of lysine, which has a positively charged side chain, and glutamate, which has a negatively charged side chain, these two amino acids are likely to form a strong ionic bond. This interaction is significant in stabilizing the protein's tertiary structure.
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Tertiary Structure of Proteins
The tertiary structure of a protein refers to its three-dimensional shape formed by the folding of its polypeptide chain. This structure is stabilized by various interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, and disulfide bridges. Understanding how specific amino acid interactions contribute to this structure is essential for grasping protein functionality.
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Related Practice
Textbook Question
What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?
b. alanine and valine
Textbook Question
What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?
d. glutamine and arginine
Textbook Question
Determine whether each of the following statements describes the primary, secondary, tertiary, or quaternary structure of a protein.
b. Peptide bonds join amino acids in a polypeptide chain.
Textbook Question
Describe the differences in the shape of an α helix and a β-pleated sheet.
Textbook Question
When a protein folds into its tertiary structure, does the primary structure change? Explain.