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Amino acids, the building blocks of proteins, can be classified based on their side chain properties, which influence their behavior and interactions in proteins. Here's a breakdown according to the categories you've asked for:
Hydrophobic Amino Acids
These amino acids have side chains that are nonpolar, making them prefer to avoid water and stay within the interior of proteins or membranes.
Alanine (Ala, A)
Isoleucine (Ile, I)
Leucine (Leu, L)
Methionine (Met, M)
Phenylalanine (Phe, F)
Proline (Pro, P)
Tryptophan (Trp, W)
Valine (Val, V)
Note: Cysteine (Cys, C) and Tyrosine (Tyr, Y) can sometimes act as hydrophobic, but their side chains have reactive groups that can also participate in polar interactions, making them borderline cases.
Hydrophilic Amino Acids
These amino acids have side chains that are polar or charged, allowing them to interact well with water.
Serine (Ser, S)
Threonine (Thr, T)
Asparagine (Asn, N)
Glutamine (Gln, Q)
Tyrosine (Tyr, Y)
Cysteine (Cys, C)
Positively Charged (Basic) Amino Acids
These amino acids have side chains that are positively charged at physiological pH, making them hydrophilic.
Lysine (Lys, K)
Arginine (Arg, R)
Histidine (His, H)
Negatively Charged (Acidic) Amino Acids
These amino acids have side chains that are negatively charged at physiological pH.
Aspartic acid (Asp, D)
Glutamic acid (Glu, E)
Non-Charged Hydrophilic Amino Acids
These amino acids are polar but do not carry a charge at physiological pH, making them hydrophilic.
Serine (Ser, S)
Threonine (Thr, T)
Asparagine (Asn, N)
Glutamine (Gln, Q)
Tyrosine (Tyr, Y)
This classification is fundamental for understanding protein structure, function, and interactions, influencing how proteins fold, how they interact with other molecules, and their roles within cells.