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Ch.18 Amino Acids and Proteins
Chapter 18, Problem 18.31

Both α-keratin and tropocollagen have helical secondary structure. How do these molecules differ in (a) amino acid composition and (b) three-dimensional structure?

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Step 1: Understand the basic structure of α-keratin and tropocollagen. α-keratin is a fibrous protein found in hair, nails, and the outer layer of skin, while tropocollagen is a precursor to collagen, which is a major component of connective tissues.
Step 2: Examine the amino acid composition of α-keratin. It is rich in cysteine, which forms disulfide bonds that contribute to its strength and rigidity.
Step 3: Analyze the amino acid composition of tropocollagen. It is characterized by a high content of glycine, proline, and hydroxyproline, which are crucial for its triple-helix structure.
Step 4: Compare the three-dimensional structure of α-keratin and tropocollagen. α-keratin forms a coiled-coil structure, where two α-helices are twisted around each other, stabilized by disulfide bonds.
Step 5: Describe the three-dimensional structure of tropocollagen. It consists of three polypeptide chains wound around each other in a triple helix, stabilized by hydrogen bonds, with glycine at every third position allowing tight packing.

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Key Concepts

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

α-Keratin

α-Keratin is a fibrous protein that primarily consists of a high proportion of hydrophobic amino acids, such as alanine, valine, and leucine. This composition contributes to its structural stability and strength, making it a key component in hair, nails, and the outer layer of skin. The helical structure of α-keratin is formed by coiling of polypeptide chains, which can aggregate into larger fibers.

Tropocollagen

Tropocollagen is the basic structural unit of collagen, characterized by a unique triple helix formation. It contains a repeating sequence of glycine, proline, and hydroxyproline, which is crucial for its stability and function in connective tissues. The triple helical structure allows tropocollagen to provide tensile strength and support in various tissues, including cartilage, bone, and skin.

Secondary and Tertiary Structure

The secondary structure of proteins refers to local folded structures that form within a polypeptide due to hydrogen bonding, such as alpha helices and beta sheets. In contrast, the tertiary structure is the overall three-dimensional shape of a protein, determined by interactions among various side chains. While both α-keratin and tropocollagen exhibit helical secondary structures, their tertiary structures differ significantly due to their distinct amino acid compositions and the nature of their interactions.
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Tertiary Protein Structure Example 1
Related Practice
Textbook Question

How many ways can four different amino acids be arranged in a peptide so that each peptide is unique?

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Textbook Question

Examine the α-helix in Figure 18.1 and determine how many backbone C and N atoms are included in the loop between an amide hydrogen atom and the carbonyl oxygen to which it is hydrogen bonded.

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Textbook Question

Consult the β-sheet in Figure 18.2 and (a) name the bonding responsible for the sheet formation and (b) identify the specific atoms responsible for this bonding.

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Textbook Question

Draw the hexapeptide Asp-Gly-Phe-Leu-Glu-Ala in linear form showing all of the atoms, and show (using dotted lines) the hydrogen bonding that stabilizes this structure if it is part of an α-helix.

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Textbook Question

Compare and contrast the characteristics of fibrous and globular proteins. Consider biological function, water solubility, amino acid composition, secondary structure, and tertiary structure. Give examples of three fibrous and three globular proteins. (Hint: Make a table.)

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Textbook Question

Cell membranes are studded with proteins. Some of these proteins, involved in the transport of molecules across the membrane into the cell, span the entire membrane and are called transmembrane proteins. The interior of the cell membrane is hydrophobic and nonpolar, whereas both the extracellular and intracellular fluids are water-based.


a. List three amino acids you would expect to find in the part of a transmembrane protein that lies within the cell membrane.

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