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Polar neutral amino acids -- hydrophilic due to a partial + or - charge that allows them to interact with water

a) Asparagine, Glutamine
b) Serine, Threonine
c) Arginine, Lysine
d) Tyrosine, Cysteine

User Peterdk
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1 Answer

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Final answer:

Polar neutral amino acids that are hydrophilic typically possess hydrophilic side chains with functional groups capable of hydrogen bonding, such as asparagine and glutamine, making them the correct answer (option a).

Step-by-step explanation:

Polar neutral amino acids are characterized by hydrophilic side chains that allow them to form hydrogen bonds with water but do not carry an overall charge. These amino acids typically have side chains with functional groups like alcohol (-OH) as found in serine and threonine, or amide (-CONH₂) as in asparagine and glutamine. Therefore, the correct answer to the question about polar neutral amino acids that are hydrophilic is option a) Asparagine, Glutamine.

Hydrophilic amino acids are soluble in water due to their capacity to engage in hydrogen bonding or ion-dipole interactions. On the other hand, hydrophobic amino acids tend to avoid water and cluster together due to their nonpolar side chains.

User Eugene Kosov
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