Textbook Question
What type of information is used to direct different polypeptides to fold into different shapes?
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Ch.3 - Protein Structure and Function
Freeman8th EditionBiological ScienceISBN: 9780138276263
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Table of contents
- Ch. 1 - Biology: The Study of Life13
- Ch. 2 - Water and Carbon: The Chemical Basis of Life14
- Ch.3 - Protein Structure and Function10
- Ch.4 - Nucleic Acids and the RNA World10
- Ch. 5 - An Introduction to Carbohydrates10
- Ch. 6 - Lipids, Membranes, and the First Cells11
- Ch. 7 - Inside the Cell10
- Ch. 8 - Energy and Enzymes: An Introduction to Metabolism10
- Ch. 9 - Cellular Respiration and Fermentation11
- Ch. 10 - Photosynthesis12
- Ch. 11 - Cell-Cell Interactions12
- Ch. 12 - The Cell Cycle8
- Ch. 13 - Meiosis12
- Ch. 14 - Mendel and the Gene23
- Ch. 15 - DNA and the Gene: Synthesis and Repair15
- Ch. 16 - How Genes Work16
- Ch. 17 - Transcription, RNA Processing, and Translation16
- Ch. 18 - Control of Gene Expression in Bacteria16
- Ch. 19 - Control of Gene Expression in Eukaryotes12
- Ch. 20 - The Molecular Revolution: Biotechnology, Genomics, and New Frontiers15
- Ch. 21 - Genes, Development, and Evolution12
- Ch. 22 - Evolution by Natural Selection16
- Ch. 23 - Evolutionary Processes13
- Ch. 24 - Speciation15
- Ch. 25 - Phylogenies and the History of Life13
- Ch. 26 - Bacteria and Archaea15
- Ch. 27 - Diversification of Eukaryotes16
- Ch. 28 - Green Algae and Land Plants16
- Ch. 29 - Fungi18
- Ch. 30 - An Introduction to Animals9
- Ch. 31 - Protostome Animals15
- Ch. 32 - Deuterostome Animals17
- Ch. 33 - Viruses16
- Ch. 34 - Plant Form and Function16
- Ch. 35 - Water and Sugar Transport in Plants16
- Ch. 36 - Plant Nutrition13
- Ch. 37 - Plant Sensory Systems, Signals, and Responses16
- Ch. 38 - Flowering Plant Reproduction and Development16
- Ch. 39 - Animal Form and Function17
- Ch. 40 - Water and Electrolyte Balance in Animals16
- Ch. 41 - Animal Nutrition16
- Ch. 42 - Gas Exchange and Circulation16
- Ch. 43 - Animal Nervous Systems16
- Ch. 44 - Animal Sensory Systems16
- Ch. 45 - Animal Movement11
- Ch. 46 - Chemical Signals in Animals16
- Ch. 47 - Animal Reproduction and Development16
- Ch. 48 - The Immune System in Animals16
- Ch. 49 - An Introduction to Ecology15
- Ch. 50 - Behavioral Ecology16
- Ch. 51 - Population Ecology16
- Ch. 52 - Community Ecology20
- Ch. 53 - Ecosystems and Global Ecology17
- Ch. 54 - Biodiversity and Conservation Ecology18
Chapter 3, Problem 6
Explain how molecular chaperones facilitate protein folding in many different polypeptides, each with their own specific shape.
Verified step by step guidance1
Molecular chaperones are specialized proteins that assist in the proper folding of other proteins without being part of the final structure. They prevent misfolding and aggregation that can lead to cell malfunction or disease.
Chaperones bind to nascent or partially folded polypeptides to stabilize them. This binding shields hydrophobic regions of the polypeptide that might otherwise clump together improperly.
The chaperones provide a secluded environment where the polypeptide can fold into its native structure without interference from other cellular components. This is crucial because the crowded environment of the cell can lead to incorrect protein interactions.
ATP provides the energy for the chaperones' function. The hydrolysis of ATP to ADP causes a conformational change in the chaperone protein, which can increase the efficiency of the folding process.
Once the protein is properly folded, the chaperone releases it. The protein can then go on to perform its specific function in the cell. This release is also ATP-dependent, ensuring that the process is tightly regulated.
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Key Concepts
Here are the essential concepts you must grasp in order to answer the question correctly.
Molecular Chaperones
Molecular chaperones are specialized proteins that assist in the proper folding of other proteins. They prevent misfolding and aggregation by binding to nascent polypeptides and stabilizing them during the folding process. Chaperones do not dictate the final structure but create an environment conducive to correct folding.
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04:00
Denatured Proteins & Chaperones
Protein Folding
Protein folding is the process by which a polypeptide chain acquires its functional three-dimensional structure. This process is driven by the sequence of amino acids and involves various interactions, such as hydrogen bonds, hydrophobic interactions, and van der Waals forces. Proper folding is crucial for protein functionality, as misfolded proteins can lead to diseases.
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08:02Protein Structure
Polypeptide Specificity
Each polypeptide has a unique sequence of amino acids that determines its specific shape and function. The diversity in polypeptide sequences leads to a wide variety of protein structures, which are essential for different biological roles. Molecular chaperones recognize and assist in the folding of these diverse polypeptides, ensuring that each achieves its correct conformation.
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Related Practice
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
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.
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Textbook Question
Predict the effect on protein function if each polypeptide adopted only a single, inflexible shape based on its primary structure.
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Textbook Question
Based on what you know of the peptide bonds that link together amino acid residues, why would proline's side chain reduce the flexibility of the backbone?
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