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

3. Amino Acids

Amino Acid Groups

Biochemistry

3. Amino Acids

Amino Acid Groups

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Multiple Choice

How do the R groups (side chains) of amino acids contribute to the overall structure of a protein?

They only provide energy for peptide bond formation and have no structural role.

They determine the folding and stability of the protein by participating in various interactions such as hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges.

They are identical in all amino acids and thus do not influence protein structure.

They are removed during protein synthesis and do not affect the final structure.

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Verified step by step guidance

Understand the role of R groups (side chains) in amino acids: R groups are the variable chemical groups attached to the alpha carbon of amino acids. These groups differ among amino acids and determine their chemical properties, such as polarity, charge, and hydrophobicity.

Learn how R groups influence protein folding: Proteins fold into specific three-dimensional structures based on interactions between amino acid side chains. These interactions include hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges.

Explore hydrogen bonding: Polar R groups can form hydrogen bonds with other polar groups or the surrounding water molecules, contributing to the stability of the protein's structure.

Examine ionic bonds and hydrophobic interactions: Charged R groups can form ionic bonds with oppositely charged groups, while nonpolar R groups cluster together to avoid water, creating hydrophobic interactions that drive protein folding.

Understand the role of disulfide bridges: Cysteine residues with thiol (-SH) groups can form covalent disulfide bonds, which provide additional stability to the protein's tertiary or quaternary structure.