Using sickle-cell anemia as an example, describe what is meant by a molecular or genetic disease. What are the similarities and dissimilarities between this type of a disorder and a disease caused by an invading microorganism?
Ch. 13 - Translation and Proteins
Chapter 13, Problem 16
In your opinion, which of the four levels of protein organization is the most critical to a protein’s function? Defend your choice.
Verified step by step guidance1
Step 1: Understand the four levels of protein structure: primary, secondary, tertiary, and quaternary. Each level describes a different aspect of the protein's shape and complexity.
Step 2: Define each level briefly: Primary structure is the linear sequence of amino acids; secondary structure involves local folding patterns like alpha-helices and beta-sheets; tertiary structure is the overall 3D shape of a single polypeptide chain; quaternary structure is the arrangement of multiple polypeptide subunits.
Step 3: Consider how each level contributes to protein function. The primary structure determines the amino acid sequence, which influences folding; secondary structures stabilize local regions; tertiary structure creates the active site and overall shape necessary for function; quaternary structure allows interaction between subunits for complex functions.
Step 4: Argue why one level might be the most critical. For example, the tertiary structure is often considered most critical because it determines the protein's specific 3D shape, which is essential for binding substrates and performing biological functions.
Step 5: Support your choice with examples or reasoning, such as how misfolding at the tertiary level can lead to loss of function or diseases, emphasizing the importance of correct 3D conformation for protein activity.
Key Concepts
Here are the essential concepts you must grasp in order to answer the question correctly.
Primary Structure of Proteins
The primary structure is the linear sequence of amino acids in a protein, held together by peptide bonds. It determines the protein’s unique identity and directly influences higher levels of structure, ultimately affecting the protein’s function.
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Tertiary Structure of Proteins
The tertiary structure refers to the overall three-dimensional folding of a single polypeptide chain, stabilized by interactions like hydrogen bonds, disulfide bridges, and hydrophobic effects. This level is crucial because it creates the specific shape necessary for the protein’s biological activity.
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Quaternary Structure of Proteins
The quaternary structure arises when multiple polypeptide chains (subunits) assemble into a functional protein complex. This organization is essential for proteins that require multiple subunits to perform their function, such as hemoglobin.
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Related Practice
Textbook Question
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Textbook Question
Assuming that each nucleotide in an mRNA is 0.34 nm long, how many triplet codes can simultaneously occupy the space in a ribosome that is 20 nm in diameter?
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Textbook Question
List as many different categories of protein functions as you can. Wherever possible, give an example of each category.
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Textbook Question
How does an enzyme function? Why are enzymes essential for living organisms on Earth?
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Textbook Question
Several amino acid substitutions in the α and β chains of human hemoglobin are shown in the following table.
Using the code table, determine how many of them can occur as a result of a single-nucleotide change.
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