Skip to main content
Ch.3 - Protein Structure and Function
Chapter 3, Problem 3

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

Verified step by step guidance
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.

Verified Solution

Video duration:
1m
This video solution was recommended by our tutors as helpful for the problem above.
Was this helpful?

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.
Recommended video:
Guided course
04:25
Community Structure

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.
Recommended video:
Guided course
04:
Denatured Proteins & Chaperones

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.
Recommended video:
Guided course
04:26
Post-Translational Modification
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 amino group and a hydroxyl group

c. an amino group and a carboxyl group

101
views
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.

734
views
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

905
views
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.

1097
views
Textbook Question

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

894
views
Textbook Question

Why are proteins not considered to be a good candidate for the first living molecule? a. Their catalytic capability is not sufficient for most biological reactions. b. Their amino acid monomers were not likely present in the prebiotic soup. c. They cannot serve as a template for replication. d. They could not have polymerized from amino acid monomers under early Earth conditions.

1348
views