Table of contents

1. Introduction to Biochemistry4h 34m
2. Water3h 23m
3. Amino Acids8h 10m
4. Protein Structure10h 4m
5. Protein Techniques14h 5m
6. Enzymes and Enzyme Kinetics13h 38m
7. Enzyme Inhibition and Regulation 8h 42m
8. Protein Function 9h 41m
9. Carbohydrates7h 49m
10. Lipids5h 49m
11. Biological Membranes and Transport 6h 37m
12. Biosignaling9h 45m
Review 1: Nucleic Acids, Lipids, & Membranes2h 47m
Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway3h 12m
Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism2h 26m
Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation1h 48m

4. Protein Structure

Peptide Bond

Biochemistry

4. Protein Structure

Peptide Bond

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Multiple Choice

Which of the following statements about peptide bonds is true?

Peptide bonds are formed by a condensation reaction between the amino group of one amino acid and the carboxyl group of another.

Peptide bonds allow free rotation around the C–N bond.

Peptide bonds are nonpolar and do not participate in hydrogen bonding.

Peptide bonds are easily hydrolyzed under physiological conditions.

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Verified step by step guidance

Step 1: Understand the nature of peptide bonds. Peptide bonds are covalent bonds formed between amino acids during protein synthesis. They are created through a condensation reaction, where a molecule of water is removed as the amino group (-NH₂) of one amino acid reacts with the carboxyl group (-COOH) of another amino acid.

Step 2: Analyze the structural properties of peptide bonds. Peptide bonds are planar and rigid due to resonance between the carbonyl oxygen and the nitrogen. This resonance restricts free rotation around the C–N bond, making the peptide bond a fixed structure.

Step 3: Evaluate the polarity and hydrogen bonding capability of peptide bonds. Peptide bonds are polar because of the partial charges on the oxygen and nitrogen atoms due to resonance. This polarity allows peptide bonds to participate in hydrogen bonding, which is crucial for protein secondary and tertiary structures.

Step 4: Assess the stability of peptide bonds under physiological conditions. Peptide bonds are relatively stable and not easily hydrolyzed under normal physiological conditions. Hydrolysis typically requires enzymatic activity or extreme conditions such as high temperature or strong acids/bases.

Step 5: Compare the given statements to the properties of peptide bonds. Based on the analysis, the correct statement is: 'Peptide bonds are formed by a condensation reaction between the amino group of one amino acid and the carboxyl group of another.' The other statements are incorrect because peptide bonds do not allow free rotation, are polar and participate in hydrogen bonding, and are not easily hydrolyzed under physiological conditions.