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Ch.3 - Protein Structure and Function
Freeman - Biological Science 7th Edition
Freeman7th EditionBiological ScienceISBN: 9783584863285Not the one you use?Change textbook
Chapter 3, Problem 3

What type of information is used to direct different polypeptides to fold into different shapes?

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1
Step 1: Understand the question. The question is asking about the information that guides the folding of polypeptides into different shapes.
Step 2: Recall that polypeptides are chains of amino acids. The sequence of these amino acids, which is determined by the sequence of nucleotides in the DNA, is what guides the folding of the polypeptide.
Step 3: Remember that the folding of a polypeptide into a specific shape is crucial for its function. This is because the shape of a protein determines its properties and functions.
Step 4: Understand that the folding process is also influenced by the cellular environment, including the presence of other molecules that can assist in the folding process.
Step 5: Summarize the answer. The sequence of amino acids in a polypeptide, which is determined by the DNA, and the cellular environment are the types of information used to direct different polypeptides to fold into different shapes.

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Key Concepts

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

Polypeptide Structure

Polypeptides are chains of amino acids that fold into specific three-dimensional shapes, which are crucial for their function. The sequence of amino acids determines how the polypeptide will fold, influenced by interactions such as hydrogen bonds, ionic bonds, and hydrophobic interactions. Understanding the primary, secondary, tertiary, and quaternary structures of proteins is essential for grasping how different shapes arise.
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Chaperone Proteins

Chaperone proteins assist in the proper folding of polypeptides into their functional shapes. They help prevent misfolding and aggregation by providing an environment conducive to correct folding. Chaperones can also refold denatured proteins, highlighting their role in maintaining cellular protein homeostasis.
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Post-Translational Modifications

Post-translational modifications (PTMs) are chemical changes that occur to polypeptides after translation, influencing their final shape and function. Common PTMs include phosphorylation, glycosylation, and methylation, which can alter the protein's properties, interactions, and stability. These modifications are critical for the regulation of protein activity and cellular signaling.
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Related Practice
Textbook Question

What two functional groups are bound to the central carbon of every free amino acid monomer?

a. An R-group and a hydroxyl group

b. An N—H group and a (C═O) group

c. An amino group and a hydroxyl group

d. An amino group and a carboxyl group

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Textbook Question
What are the defining characteristics of a condensation reaction?a. Two monomers are covalently bonded together and a water molecule is produced.b. Two monomers are covalently bonded together and a water molecule is used up.c. A polymer is broken down into monomers and a water molecule is produced.d. A polymer is broken down into monomers and a water molecule is used up.
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Textbook Question

What type of bond is directly involved in the formation of an α-helix?

a. Peptide bonds between amino acid residues

b. Hydrogen bonds between amino acid residues

c. Van der Waals interactions between nonpolar residues

d. Disulfide bonds between cysteine residues

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Textbook Question

Which of the following correctly describe an active site? Select True or False for each statement.

T/F It is the location in an enzyme where substrates bind.

T/F It is the place where a molecule or ion binds to an inactive enzyme to induce a shape change to make it active.

T/F It is the portion of an enzyme where chaperones bind to help enzymes fold.

T/F It is the site on an enzyme where catalysis occurs.

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Textbook Question

If a cell were to use only 10 of the 20 possible amino acids, how much effect would you expect this to have on protein diversity? Calculate and compare the number of different sequences that can be generated by randomly assembling either 10 or 20 amino acids into peptides that are five residues long.

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Textbook Question

Explain how molecular chaperones facilitate protein folding in many different polypeptides, each with their own specific shape.

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