Domanda del libro di testo
What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?
b. leucine and isoleucine
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Ch.10 Proteins Workers of the Cell
Frost4th EditionGeneral, Organic and Biological ChemistryISBN: 9780134988696
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TOC.tableOfContents
- Ch.4 Introduction to Organic Compounds75
- Ch.5 Chemical Reactions19
- Ch.6 Carbohydrates Life's Sweet Molecules62
- Ch.7 States of Matter and Their Attractive Forces8
- Ch.8 Solution Chemistry Sugar and Water Do Mix4
- Ch.10 Proteins Workers of the Cell89
- Ch.11 Nucleic Acids Big Molecules with a Big Role69
- Ch.12 Food as Fuel An Overview of Metabolism65
Frost4th EditionGeneral, Organic and Biological ChemistryISBN: 9780134988696Non è quello che usi tu?Cambia libro di testo
Capitolo 6, Problema 25
Describe the differences in the shape of an α helix and a β-pleated sheet.
Guida verificata passo dopo passo1
Understand that both α helix and β-pleated sheet are types of secondary structures found in proteins, stabilized by hydrogen bonds.
Recognize that an α helix is a right-handed coil or spiral structure, where the backbone of the polypeptide chain forms the inner part of the helix and the side chains extend outward.
Note that in an α helix, hydrogen bonds form between the carbonyl oxygen of one amino acid and the amide hydrogen of an amino acid four residues earlier, creating a tightly packed structure.
Identify that a β-pleated sheet consists of two or more polypeptide chains (or segments of a single chain) aligned next to each other, forming a sheet-like structure.
Observe that in a β-pleated sheet, hydrogen bonds form between the carbonyl oxygen of one chain and the amide hydrogen of an adjacent chain, resulting in a zigzag or pleated appearance.
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α Helix Structure
The α helix is a common secondary structure in proteins characterized by a right-handed coil or spiral. Each turn of the helix typically consists of about 3.6 amino acids, with hydrogen bonds forming between the carbonyl oxygen of one amino acid and the amide hydrogen of another, four residues down the chain. This structure provides stability and is often found in fibrous proteins.
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3:27
DNA Double Helix Concept 1
β-Pleated Sheet Structure
The β-pleated sheet is another type of secondary structure in proteins, formed by linking two or more strands of amino acids through hydrogen bonds. These strands can be parallel or antiparallel, creating a sheet-like appearance. The pleated nature allows for a more extended conformation, contributing to the overall stability and functionality of the protein.
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2:42Beta-Pleated Sheet Concept 4
Hydrogen Bonding in Protein Structures
Hydrogen bonding is a crucial interaction that stabilizes both α helices and β-pleated sheets in protein structures. In α helices, hydrogen bonds form within the same strand, while in β-pleated sheets, they occur between different strands. This bonding is essential for maintaining the three-dimensional shape of proteins, influencing their biological activity and interactions.
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1:47Summary of Protein Structure Example 1
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Name the stabilizing attractive force found in secondary structures of proteins.
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Domanda del libro di testo
What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?
b. alanine and valine
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How many different tripeptides that contain one leucine, one glutamate, and one tryptophan are possible?
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What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?
a. lysine and glutamate
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When a protein folds into its tertiary structure, does the primary structure change? Explain.
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