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

Altering Primary Protein Structure

Biochemistry

4. Protein Structure

Altering Primary Protein Structure

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Multiple Choice

Which amino acid is least likely to alter protein shape/function if substituted with an Arg residue?

Lys

Tyr

Asn

Ala

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Verified step by step guidance

Identify the properties of the amino acid Arginine (Arg). Arginine is a positively charged, polar amino acid with a long side chain.

Consider the properties of each amino acid option: Lysine (Lys), Tyrosine (Tyr), Asparagine (Asn), and Alanine (Ala).

Lysine (Lys) is similar to Arginine as it is also a positively charged, polar amino acid with a long side chain, making it more likely to substitute without altering protein shape/function.

Tyrosine (Tyr) is a polar amino acid but has a bulky aromatic side chain, which differs significantly from Arginine.

Asparagine (Asn) is polar but uncharged, and Alanine (Ala) is nonpolar with a small side chain, both differing from Arginine in charge and/or size, making them less likely to substitute without altering protein shape/function.