Table of contents

1. Matter and Measurements4h 31m
2. Atoms and the Periodic Table5h 23m
3. Ionic Compounds2h 18m
4. Molecular Compounds2h 18m
5. Classification & Balancing of Chemical Reactions3h 17m
6. Chemical Reactions & Quantities2h 27m
7. Energy, Rate and Equilibrium3h 46m
8. Gases, Liquids and Solids3h 25m
9. Solutions4h 10m
10. Acids and Bases3h 29m
11. Nuclear Chemistry56m
BONUS: Lab Techniques and Procedures1h 38m
BONUS: Mathematical Operations and Functions47m
12. Introduction to Organic Chemistry1h 34m
13. Alkenes, Alkynes, and Aromatic Compounds2h 12m
14. Compounds with Oxygen or Sulfur1h 6m
15. Aldehydes and Ketones1h 1m
16. Carboxylic Acids and Their Derivatives1h 11m
17. Amines39m
18. Amino Acids and Proteins1h 51m
19. Enzymes1h 37m
20. Carbohydrates1h 41m
21. The Generation of Biochemical Energy2h 8m
22. Carbohydrate Metabolism2h 22m
23. Lipids2h 26m
24. Lipid Metabolism1h 45m
25. Protein and Amino Acid Metabolism1h 37m
26. Nucleic Acids and Protein Synthesis2h 54m

18. Amino Acids and Proteins

Secondary Protein Structure

GOB Chemistry

18. Amino Acids and Proteins

Secondary Protein Structure

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Problem 24

Textbook Question

Consult the β-sheet in Figure 18.2 and (a) name the bonding responsible for the sheet formation and (b) identify the specific atoms responsible for this bonding.

Verified step by step guidance

Step 1: Understand the structure of a β-sheet. A β-sheet is a common secondary structure in proteins, formed by the alignment of polypeptide chains in a sheet-like arrangement.

Step 2: Identify the type of bonding responsible for the formation of the β-sheet. The bonding involved is hydrogen bonding, which occurs between the backbone atoms of the polypeptide chains.

Step 3: Recognize the specific atoms involved in the hydrogen bonding. In a β-sheet, the hydrogen bonds form between the carbonyl oxygen (C=O) of one amino acid and the amide hydrogen (N-H) of another amino acid in a neighboring chain.

Step 4: Note the orientation of the β-sheet. The polypeptide chains can be arranged in either a parallel or antiparallel configuration, which affects the alignment of the hydrogen bonds.

Step 5: Summarize the findings. The bonding responsible for β-sheet formation is hydrogen bonding, and the specific atoms involved are the carbonyl oxygen and the amide hydrogen from the peptide backbone.

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Key Concepts

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

β-sheet Structure

The β-sheet is a common secondary structure in proteins, characterized by strands of amino acids linked together by hydrogen bonds. These strands can be parallel or antiparallel, influencing the overall stability and properties of the protein. Understanding the arrangement of these strands is crucial for grasping how proteins fold and function.

Hydrogen Bonding

Hydrogen bonds are weak interactions that occur when a hydrogen atom covalently bonded to an electronegative atom, like oxygen or nitrogen, is attracted to another electronegative atom. In the context of β-sheets, these bonds form between the carbonyl oxygen of one amino acid and the amide hydrogen of another, stabilizing the sheet structure. This bonding is essential for maintaining the integrity of protein structures.

Amino Acid Residues

Amino acid residues are the building blocks of proteins, each consisting of an amino group, a carboxyl group, and a unique side chain. In β-sheets, specific atoms from the backbone of these residues, particularly the carbonyl (C=O) and amide (N-H) groups, participate in hydrogen bonding. Identifying these residues is key to understanding the formation and stability of the β-sheet.

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Related Practice

Textbook Question

Complete the following two sentences with either globular or fibrous:

a. Proteins with secondary structure composed primarily of alpha-helix are___________ proteins.

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Multiple Choice

How many hydrogen bonding pairs are possible when the following two peptides interact?

Which of the following statements is true in regard to the peptide strand shown?

Examine the α-helix in Figure 18.1 and determine how many backbone C and N atoms are included in the loop between an amide hydrogen atom and the carbonyl oxygen to which it is hydrogen bonded.

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Textbook Question

Draw the hexapeptide Asp-Gly-Phe-Leu-Glu-Ala in linear form showing all of the atoms, and show (using dotted lines) the hydrogen bonding that stabilizes this structure if it is part of an α-helix.

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Textbook Question

Compare and contrast the characteristics of fibrous and globular proteins. Consider biological function, water solubility, amino acid composition, secondary structure, and tertiary structure. Give examples of three fibrous and three globular proteins. (Hint: Make a table.)

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Textbook Question

Bradykinin, a peptide that helps to regulate blood pressure, has the primary structure Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg.

b. Bradykinin has a very kinked secondary structure. Why?

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Textbook Question

What happens when a primary structure forms a secondary structure?

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