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Ch.16 Amino Acids, Proteins, and Enzymes
Timberlake - Chemistry: An Introduction to General, Organic, and Biological Chemistry 14th Edition
Timberlake14thChemistry: An Introduction to General, Organic, and Biological ChemistryISBN: 9781292472249Not the one you use?Change textbook
All textbooksTimberlake 14thCh.16 Amino Acids, Proteins, and EnzymesProblem 81d
Chapter 16, Problem 81d

Consider the amino acids lysine, valine, and aspartate in an enzyme. State which of these amino acids have R groups that would:
d. form salt bridges

Verified step by step guidance
1
Understand the concept of salt bridges: Salt bridges are ionic interactions that occur between oppositely charged R groups of amino acids in proteins. These interactions typically involve acidic and basic side chains.
Identify the amino acids provided: Lysine, valine, and aspartate. Examine their R groups to determine if they can participate in salt bridge formation.
Analyze lysine: Lysine has a basic R group with an amino group (-NH3+) that can carry a positive charge at physiological pH, making it capable of forming salt bridges with negatively charged groups.
Analyze aspartate: Aspartate has an acidic R group with a carboxylate group (-COO-) that carries a negative charge at physiological pH, allowing it to form salt bridges with positively charged groups.
Analyze valine: Valine has a nonpolar, hydrophobic R group (an isopropyl group) that does not carry a charge and therefore cannot participate in salt bridge formation.

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Key Concepts

Here are the essential concepts you must grasp in order to answer the question correctly.

Amino Acid R Groups

Amino acids have unique side chains, known as R groups, that determine their chemical properties and interactions. These R groups can be polar, nonpolar, acidic, or basic, influencing how amino acids behave in proteins. Understanding the nature of these R groups is essential for predicting interactions such as salt bridge formation.
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Amino Acid Catabolism: Amino Group Concept 2

Salt Bridges

Salt bridges are non-covalent interactions that occur between positively and negatively charged R groups of amino acids. They play a crucial role in stabilizing protein structures and are particularly important in enzyme function. In the context of lysine, valine, and aspartate, identifying which amino acids can form these interactions is key to understanding their roles in enzymatic activity.
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Acidic and Basic Amino Acids

Amino acids can be classified as acidic or basic based on the nature of their R groups. Aspartate is an acidic amino acid with a negatively charged side chain, while lysine is a basic amino acid with a positively charged side chain. Valine, being nonpolar, does not participate in salt bridge formation, making the distinction between these classifications vital for answering the question.
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Related Practice
Textbook Question

If a blood test indicates a high level of ALT, what could be the cause?

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Textbook Question

Consider the amino acids lysine, valine, and aspartate in an enzyme. State which of these amino acids have R groups that would:

b. be found in hydrophilic regions

Textbook Question

Consider the amino acids lysine, valine, and aspartate in an enzyme. State which of these amino acids have R groups that would:

c. form hydrogen bonds

Textbook Question

Consider the amino acids histidine, phenylalanine, and serine in an enzyme. State which of these amino acids have R groups that would:

d. form salt bridges