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

At which position(s) in a polypeptide are amino acids limited to those with positively charged side chains?

At the N-terminus only

At positions involved in forming salt bridges with negatively charged residues

At all positions within the polypeptide chain

At the C-terminus only

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Verified step by step guidance

Understand the context of the question: Amino acids with positively charged side chains include lysine (Lys), arginine (Arg), and histidine (His). These amino acids are involved in electrostatic interactions, such as salt bridges, with negatively charged residues like aspartate (Asp) and glutamate (Glu).

Review the structure of a polypeptide chain: A polypeptide has an N-terminus (amino group), a C-terminus (carboxyl group), and a sequence of amino acids in between. The side chains of amino acids in the chain determine their chemical properties and interactions.

Consider the role of positively charged amino acids: These amino acids are not restricted to specific positions like the N-terminus or C-terminus. Instead, they can be found throughout the polypeptide chain, where they participate in interactions such as salt bridges with negatively charged residues.

Analyze the concept of salt bridges: Salt bridges are formed when positively charged side chains interact with negatively charged side chains. These interactions stabilize the protein structure and can occur at any position within the polypeptide chain, depending on the protein's folding and environment.

Conclude that positively charged amino acids are not limited to specific positions like the N-terminus or C-terminus. They are distributed throughout the polypeptide chain and are involved in forming salt bridges with negatively charged residues wherever such interactions are required for structural stability or function.