Domanda del libro di testo
Why do enzymes function only under mild conditions?
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Ch.16 Amino Acids, Proteins, and Enzymes
Timberlake13th EditionChemistry: An Introduction to General, Organic, and Biological ChemistryISBN: 9780134421353
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TOC.tableOfContents
- Ch.1 Chemistry in Our Lives11
- Ch.2 Chemistry and Measurements80
- Ch.3 Matter and Energy54
- Ch.4 Atoms and Elements51
- Ch.5 Nuclear Chemistry42
- Ch.6 Ionic and Molecular Compounds57
- Ch.7 Chemical Quantities and Reactions41
- Ch.8 Gases29
- Ch.9 Solutions51
- Ch.10 Acids and Bases and Equilibrium65
- Ch.11 Introduction to Organic Chemistry: Hydrocarbons78
- Ch.12 Alcohols, Thiols, Ethers, Aldehydes, and Ketones83
- Ch.13 Carbohydrates54
- Ch.14 Carboxylic Acids, Esters, Amines, and Amides90
- Ch.15 Lipids61
- Ch.16 Amino Acids, Proteins, and Enzymes84
- Ch.17 Nucleic Acids and Protein Synthesis83
- Ch.18 Metabolic Pathways and ATP Production67
Timberlake13th EditionChemistry: An Introduction to General, Organic, and Biological ChemistryISBN: 9780134421353Non è quello che usi tu?Cambia libro di testo
Capitolo 16, Problema 66b
What are some differences between each of the following pairs?
b. an ⍺ helix and collagen
Guida verificata passo dopo passo1
Understand the context: Both α helix and collagen are structural components of proteins, but they differ in their structure and function. The α helix is a common secondary structure in proteins, while collagen is a fibrous protein with a unique triple-helix structure.
Step 1: Describe the α helix. The α helix is a right-handed helical structure stabilized by hydrogen bonds between the carbonyl oxygen of one amino acid and the amide hydrogen of another amino acid four residues away. This structure is compact and found in globular proteins.
Step 2: Describe collagen. Collagen is a fibrous protein that forms a triple helix, consisting of three polypeptide chains wound around each other. It is rich in glycine, proline, and hydroxyproline, which contribute to its strength and stability. Collagen is a major component of connective tissues like tendons, ligaments, and skin.
Step 3: Highlight the differences in structure. The α helix is a single polypeptide chain with intrachain hydrogen bonding, while collagen consists of three polypeptide chains with interchain hydrogen bonding. Additionally, the α helix is more flexible, whereas collagen is rigid and provides tensile strength.
Step 4: Highlight the differences in function. The α helix is typically found in globular proteins and contributes to their dynamic roles, such as enzyme activity or transport. Collagen, on the other hand, is a structural protein that provides support and strength to tissues.
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α Helix Structure
The α helix is a common structural motif in proteins, characterized by a right-handed coil where each turn of the helix contains about 3.6 amino acids. This structure is stabilized by hydrogen bonds between the backbone amide and carbonyl groups, contributing to the overall stability and functionality of proteins. The α helix is crucial for the secondary structure of proteins and plays a significant role in their biological activity.
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DNA Double Helix Concept 1
Collagen Structure
Collagen is a fibrous protein that forms a triple helix structure, consisting of three polypeptide chains wound around each other. This unique structure provides tensile strength and is a major component of connective tissues, such as skin, tendons, and cartilage. Unlike the α helix, collagen's stability is enhanced by cross-linking between the chains, making it essential for structural integrity in various biological tissues.
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Functional Differences
The functional differences between an α helix and collagen arise from their distinct structures. The α helix is often involved in the active sites of enzymes and plays a role in protein interactions, while collagen primarily provides structural support and strength to tissues. These differences in function are a direct result of their unique structural properties, influencing how they contribute to the overall physiology of organisms.
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02:16Logarithmic Functions
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