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Ch.10 Proteins Workers of the Cell
Frost - General, Organic and Biological Chemistry 4th Edition
Frost4th EditionGeneral, Organic and Biological ChemistryISBN: 9780134988696Not the one you use?Change textbook
Chapter 6, Problem 30a

Myoglobin is a protein containing 153 amino acids. Approximately half of the amino acids in myoglobin have polar side chains.
a. Where would you expect these amino acid side chains to be located in the tertiary structure of the protein?

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1
Understand the structure of myoglobin: Myoglobin is a globular protein, which means it has a compact, spherical shape.
Recognize the nature of polar side chains: Polar side chains are hydrophilic, meaning they are attracted to water.
Consider the environment of myoglobin: In an aqueous environment, such as the cytoplasm of a cell, proteins like myoglobin are surrounded by water.
Predict the location of polar side chains: In the tertiary structure of myoglobin, polar side chains are likely to be located on the exterior surface of the protein, where they can interact with the surrounding water molecules.
Contrast with non-polar side chains: Non-polar side chains, which are hydrophobic, tend to be located in the interior of the protein, away from water.

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Key Concepts

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

Tertiary Structure of Proteins

The tertiary structure of a protein refers to its three-dimensional shape formed by the folding of the polypeptide chain. This structure is stabilized by various interactions, including hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges. Understanding the tertiary structure is crucial for predicting how a protein will function and interact with other molecules.
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Polar and Nonpolar Amino Acids

Amino acids can be classified based on the properties of their side chains as polar or nonpolar. Polar amino acids have side chains that can form hydrogen bonds with water, making them hydrophilic, while nonpolar amino acids have hydrophobic side chains that do not interact favorably with water. The distribution of these amino acids in a protein's structure influences its folding and stability.
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Hydrophobic Effect

The hydrophobic effect is a key driving force in protein folding, where nonpolar side chains tend to cluster away from the aqueous environment, while polar side chains are oriented towards the surface. This phenomenon helps stabilize the protein's tertiary structure by minimizing the exposure of hydrophobic regions to water, thus influencing the overall conformation and functionality of the protein.
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