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Ch.18 Amino Acids and Proteins
McMurry - Fundamentals of General, Organic, and Biological Chemistry 8th Edition
McMurry8th EditionFundamentals of General, Organic, and Biological ChemistryISBN: 9780134015187당신이 사용하는 게 아니라요?교과서 변경
18장, 문제 109

Which would you expect to be more soluble in water, a peptide containing mostly alanine and leucine or a peptide containing mostly lysine and aspartic acid? Explain. (Hint: Consider side-chain interactions with water.)

검증된 단계별 안내
1
Step 1: Understand the nature of the side chains of the amino acids involved. Alanine and leucine have nonpolar, hydrophobic side chains, while lysine has a positively charged (basic) side chain and aspartic acid has a negatively charged (acidic) side chain.
Step 2: Recall that water is a polar solvent, meaning it interacts more favorably with polar or charged molecules through hydrogen bonding and dipole-dipole interactions.
Step 3: Analyze the peptide containing alanine and leucine. Since these amino acids have nonpolar side chains, the peptide will have limited interactions with water, making it less soluble.
Step 4: Analyze the peptide containing lysine and aspartic acid. These amino acids have charged side chains, which can form strong electrostatic interactions and hydrogen bonds with water, increasing the peptide's solubility.
Step 5: Conclude that the peptide containing mostly lysine and aspartic acid would be more soluble in water due to the polar and charged nature of their side chains, which interact favorably with water molecules.

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주요 개념

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Polarity of Amino Acids

Amino acids have varying side chains that can be polar or nonpolar. Polar amino acids, like lysine and aspartic acid, interact favorably with water due to their ability to form hydrogen bonds. In contrast, nonpolar amino acids, such as alanine and leucine, do not interact well with water, making them less soluble.
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가이드 코스
2:55
Polar Amino Acids Concept 2

Hydrophilicity vs. Hydrophobicity

Hydrophilicity refers to the affinity of a substance for water, while hydrophobicity indicates a lack of such affinity. Peptides with hydrophilic side chains, like those containing lysine and aspartic acid, tend to dissolve better in water compared to those with hydrophobic side chains, such as alanine and leucine.
추천 영상:
가이드 코스
3:33
Enantiomers vs Diastereomers Concept 1

Ionic and Hydrogen Bonding

Ionic and hydrogen bonds are crucial for solubility in water. Amino acids like lysine, which has a positively charged side chain, can form ionic bonds with negatively charged water molecules. Similarly, aspartic acid can form hydrogen bonds, enhancing the solubility of peptides rich in these amino acids compared to those with nonpolar residues.
추천 영상:
가이드 코스
02:33
Ionic Bonding Concept 1
관련 실천
교과서 질문

Globular proteins are water-soluble, whereas fibrous proteins are insoluble in water. Indicate whether you expect the following amino acids to be on the surface of a globular protein or on the surface of a fibrous protein.

a. Ala

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교과서 질문

Which of the following amino acids is most likely to be found on the outside of a soluble protein, and which of them is more likely to be found on the inside? Explain each answer. (Hint: Consider the effect of the amino acid side chain in each case and that the protein is folded up into its globular form.)

a. Valine

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교과서 질문

Four of the most abundant amino acids in proteins are leucine, alanine, glycine, and valine. What do these amino acids have in common? Would you expect these amino acids to be found on the interior or on the exterior of the protein?

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교과서 질문

A family visits a pediatrician with their sick child. The four-month-old baby is pale, has obvious episodes of pain, and is not thriving. The doctor orders a series of blood tests, including a test for hemoglobin types. The results show that the infant is not only anemic but that the anemia is due to sickle-cell anemia. The family wants to know if their other two children have sickle-cell anemia, sickle-cell trait, or no sickle-cell gene at all.

a. What test will be used?

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교과서 질문

List the amino acids with side chains that are capable of hydrogen bonding. Draw an example of two of these amino acids hydrogen bonding to one another. For each one, draw a hydrogen bond to water in a separate sketch. Refer to Section 8.2 for help with drawing hydrogen bonds.

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