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Ch.16 Amino Acids, Proteins, and Enzymes
Timberlake - Chemistry: An Introduction to General, Organic, and Biological Chemistry 13th Edition
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.

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1
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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