The folding of a polypeptide chain depends not only on its amino acid sequence but also on the nature of the solvent. Discuss the types of interactions that might occur between water molecules and the amino acid residues of the polypeptide chain. Which groups would be exposed on the exterior of the protein in contact with water and which groups would be buried in the interior of the protein?

Short Answer

Expert verified
Water interacts with the polypeptide chain via ionic and hydrogen bonding, van der Waals forces, and hydrophobic interactions. Polar and charged amino acid residues are generally located on the exterior of the protein, in contact with water as they can form favorable interactions. On the other hand, hydrophobic residues are most likely found in the interior of the protein as they can't interact favorably with water.

Step by step solution

01

Protein Structure and Interactions

The folding of a polypeptide chain is determined by the amino acid sequence and the external environment. This is mainly due to the interaction between the polypeptide and its surroundings which include the solvent. A common solvent is water. The types of interactions these molecules can have with water include ionic and hydrogen bonding, van der Waals forces, and hydrophobic interactions.
02

Exposure of Amino Acid residues

On the outer surface of the protein, interacting with water, are likely to be polar and charged amino acid residues. This is because these residues can form hydrogen bonds with water molecules (for polar residues) or interact electrostatically with water (for charged residues). Examples of such residues include Lysine, Arginine, Glutamic acid, Aspartic acid, and Histidine among others.
03

Interior of Protein

Residues buried in the interior of the protein, away from the solvent, are generally hydrophobic. They cannot form favorable interactions with water and therefore, tend to be sequestered away in the interior of the protein. Examples of these residues include Alanine, Valine, Leucine, Isoleucine, Methionine, and Phenylalanine among others.

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