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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
All textbooksFrost 4th EditionCh.10 Proteins Workers of the CellProblem 67b
Chapter 6, Problem 67b

Would you expect to find this segment at the center or on the surface of a globular protein? Why?

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Identify the segment in question and determine its chemical properties, such as whether it is hydrophobic (nonpolar) or hydrophilic (polar). This is crucial because the location of the segment in a globular protein depends on its polarity.
Recall that globular proteins are typically folded in such a way that hydrophobic (nonpolar) regions are buried in the interior (center) of the protein, away from water, while hydrophilic (polar) regions are exposed on the surface, interacting with the aqueous environment.
Analyze the amino acid composition of the segment. If the segment contains mostly nonpolar amino acids (e.g., leucine, valine, phenylalanine), it is likely to be found in the center of the protein. If it contains mostly polar or charged amino acids (e.g., serine, lysine, glutamate), it is likely to be on the surface.
Consider the role of hydrogen bonding and ionic interactions. Polar amino acids on the surface can form hydrogen bonds or ionic interactions with water or other molecules, stabilizing the protein structure in an aqueous environment.
Conclude the reasoning based on the segment's properties. For example, if the segment is hydrophobic, it would be expected to be at the center of the globular protein to avoid water, whereas a hydrophilic segment would be on the surface to interact with water.

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Key Concepts

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

Globular Proteins

Globular proteins are spherical in shape and are typically soluble in water. They play crucial roles in biological processes, including enzyme activity, transport, and immune responses. Their structure allows for a diverse range of functions, as the folding of the protein creates specific active sites and binding pockets.
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Digestion of Proteins Concept 1

Hydrophobic and Hydrophilic Interactions

In globular proteins, amino acids can be classified as hydrophobic (water-repelling) or hydrophilic (water-attracting). Hydrophobic amino acids tend to be found in the interior of the protein, away from water, while hydrophilic amino acids are usually located on the surface, interacting with the aqueous environment. This distribution is crucial for the protein's stability and function.
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Interactions within the Tertiary Structure Concept 2

Protein Folding

Protein folding is the process by which a linear chain of amino acids acquires its functional three-dimensional structure. This process is driven by various interactions, including hydrogen bonds, ionic bonds, and van der Waals forces. Proper folding is essential for the protein's functionality, and misfolding can lead to diseases.
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Tertiary Protein Structure Example 1
Related Practice
Textbook Question

Identify the level of protein structure associated with each of the following:

b. hydrogen bonding between backbone atoms

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Textbook Question

Consider the amino acids glycine, proline, and lysine.

b. Using three-letter abbreviations for the amino acids, give the sequence for each of the possible tripeptides.

Textbook Question

Identify some differences between the following pairs:

b. complete and incomplete proteins

Textbook Question

Name the covalent bond that helps to stabilize the tertiary structure of a protein.

Textbook Question

Draw the structure of the possible dipeptides formed from one alanine combining with one cysteine.

Textbook Question

Aspartame, which is commonly known as NutraSweet™, contains the following dipeptide:

d. Draw the structure of the isomer of this dipeptide where the C-terminal and N-terminal amino acids are switched.