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

Previous problemNext problem

Struggling with Biochemistry?

Join thousands of students who trust us to help them ace their exams!Watch the first video

Multiple Choice

How do the side chains (R groups) of amino acids influence the structure and function of proteins?

They serve solely as energy sources and are not involved in protein function.

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

They only affect the primary sequence of proteins and have no impact on higher-order structures.

They determine the folding, stability, and interactions of proteins by contributing specific chemical properties such as charge, hydrophobicity, and hydrogen bonding.

Previous problemNext problem

Verified step by step guidance

Step 1: Understand the role of amino acid side chains (R groups). Amino acids are the building blocks of proteins, and their side chains contribute unique chemical properties such as charge, hydrophobicity, and ability to form hydrogen bonds.

Step 2: Recognize how these chemical properties influence protein folding. Proteins fold into specific three-dimensional structures based on interactions between amino acid side chains, including hydrophobic interactions, ionic bonds, and hydrogen bonds.

Step 3: Explore the impact on protein stability. The side chains help stabilize the protein structure by forming interactions that minimize free energy, such as hydrophobic residues clustering away from water and charged residues forming salt bridges.

Step 4: Examine the role in protein function. The chemical properties of side chains determine how proteins interact with other molecules, such as substrates, cofactors, or other proteins, enabling specific biological functions.

Step 5: Clarify misconceptions. Side chains are not removed during protein synthesis, nor do they solely affect the primary sequence. Instead, they play a critical role in determining higher-order structures (secondary, tertiary, and quaternary) and overall protein functionality.