In a normal cellular protein, where would you expect to find a hydrophilic amino acid such as asparagine? in a normal cellular protein, where would you expect to find a hydrophilic amino acid such as asparagine? on the exterior surface of the protein, interacting with water, or in a transmembrane portion interacting with lipid fatty acid chains in the transmembrane portion interacting with lipid fatty acid chains in the interior of the folded protein, away from water on the exterior surface of the protein, interacting with water

In a normal cellular protein, it is expected to observe hydrophilic amino acids (e.g., asparagine) on the EXTERIOR surface of the protein, INTERACTING with water.

Hydrophilic amino acids (i.e., serine, threonine, cysteine, asparagine, and glutamine) are amino acids that attract water molecules due to their polar properties.

These hydrophilic amino acids have R (lateral) groups that can form hydrogen bonds with water.

For example, Asparagine (Asn) is a hydrophilic and polar amino acid because this residue can form hydrogen bonds through its hydroxyl (OH) and amide (NH) groups.

In conclusion, in a normal cellular protein, it is expected to observe hydrophilic amino acids (e.g., asparagine) on the EXTERIOR surface of the protein, INTERACTING with water.

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The answer to your question is:

Explanation:

A hydrophillic protein, is a protein that can dissolve or be in contact with water.

Asparagine is a non-essential aminoacid that has a carboxiamide group , one carboxy group and one amino group.

According with this information, we can conclude that asparagine is found on the exterior surface of the protein, interacting with water.

electron microscopy and scanning tunneling microscopes gives us a greater understanding of atoms by being able to see the atom itself, and lets us see some atomic reactions.

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