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

Highlight the peptide bonds in the figure below & circle all the α-carbons. How many peptide bonds are there?

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Identify the peptide bonds in the structure. A peptide bond is formed between the carboxyl group of one amino acid and the amino group of another. Look for the C=O and N-H linkage between two amino acids.

Count the number of peptide bonds. Start from the N-terminus and move towards the C-terminus, identifying each peptide bond between consecutive amino acids.

Locate the α-carbons in the structure. The α-carbon is the central carbon atom in each amino acid, bonded to the amino group, carboxyl group, hydrogen atom, and the R group.

Circle each α-carbon in the structure. Ensure that you have circled one α-carbon per amino acid residue.

Verify the number of peptide bonds and α-carbons. The number of peptide bonds should be one less than the number of amino acids, as each bond connects two amino acids.