1.6-1.7 Nucleic Acids & Proteins

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Last updated 4:25 PM on 9/3/26
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10 Terms

1
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What chemical feature distinguishes hydrophobic amino acid R groups from hydrophilic ones?

Hydrophobic R groups consist mostly of nonpolar hydrocarbons (C and H), while hydrophilic R groups contain electronegative atoms (O, N) or charges.

2
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Which amino acid has an R group consisting of only a single hydrogen atom?

Glycine (Gly, G).

3
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Which amino acid forms covalent disulfide bridges through its sulfur-containing R group?

Cysteine (Cys, C).

4
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What unique structural property does the special amino acid Proline have?

Its R group forms a ring structure that loops back and connects to its own amino group backbone.

5
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What charge do acidic amino acid R groups carry at biological pH, and which two amino acids belong to this group?

They carry a negative charge (-); examples are Aspartic acid (Asp, D) and Glutamic acid (Glu, E).

6
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What charge do basic amino acid R groups carry at biological pH, and which three amino acids belong to this group?

They carry a positive charge (+); examples are Lysine (Lys, K), Arginine (Arg, R), and Histidine (His, H).

7
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In secondary structure, which specific atoms form the hydrogen bonds that stabilize alpha-helices and beta-pleated sheets?

Hydrogen bonds form between the oxygen of a carbonyl group (C=O) and the hydrogen of an amine group (N-H) along the polypeptide backbone.

8
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What role do R groups play in forming secondary protein structures?

None—secondary structure is stabilized entirely by hydrogen bonding along the peptide backbone, regardless of the R groups.

9
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What four types of interactions between R groups drive tertiary structure folding?

1) Hydrogen bonding between polar R groups, 2) Charge attractions (ionic bonds) between acidic (-) and basic (+) R groups, 3) Hydrophobic interactions/collapse, and 4) Covalent disulfide bridges between cysteines.

10
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Which tertiary structure interaction is the strongest and why?

Disulfide bridges, because they are strong covalent bonds between sulfur atoms in cysteine side chains.