Which of the following amino acids is most likely to be...

Name: Problem 111, Chapter 18: Fundamentals of General, Organic, and Biological Chemistry
Uploaded: 2022-01-23T05:04:43-08:00
Duration: 3 min 2 s
Channel: Ramesh Singh
Description: Which of the following amino acids is most likely to be found on the outside of a soluble protein? Which is more likely to be found on the inside? Explain each answer. (Hint: Consider the effect of the amino acid side chain in each case and that the protein is folded up into its globular form.) (a) Leucine (b) Glutamate (c) Phenylalanine (d) Glutamine

Which of the following amino acids is most likely to be found on the outside of a soluble protein? Which is more likely to be found on the inside? Explain each answer. (Hint: Consider the effect of the amino acid side chain in each case and that the protein is folded up into its globular form.) (a) Leucine (b) Glutamate (c) Phenylalanine (d) Glutamine

Which of the following amino acids is most likely to be found on the outside of a soluble protein? Which is more likely to be found on the inside? Explain each answer. (Hint: Consider the effect of the amino acid side chain in each case and that the protein is folded up into its globular form.)
(a) Leucine
(b) Glutamate
(c) Phenylalanine
(d) Glutamine

Key Concepts

Amino Acid Polarity

This concept refers to the distribution of electrical charge over the atoms in an amino acid, particularly within its side chain. Polar amino acids, which can be charged or uncharged, have side chains that interact favorably with water, making them more likely to be exposed on the surface of soluble proteins. Nonpolar (hydrophobic) amino acids have side chains that do not interact with water, often leading them to be buried in the inner core of a protein where they can avoid contact with the aqueous environment.

Hydrophobic Effect

The hydrophobic effect is a fundamental driving force behind the folding of proteins. It describes the tendency of nonpolar side chains to aggregate and minimize their exposure to the polar environment of water. This effect leads to the sequestration of hydrophobic residues inside the protein’s interior, stabilizing its globular structure and contributing to its proper function.

Protein Folding and Structure

Protein folding refers to the process by which a protein assumes its functional three-dimensional structure, driven by interactions among its amino acids. In globular proteins, the arrangement of polar and nonpolar amino acids is crucial. Polar, hydrophilic side chains generally reside on the outside to interact with the surrounding aqueous milieu, while nonpolar, hydrophobic side chains are typically found on the inside, forming a stable core. This organization is essential for the protein's solubility and structural integrity.

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