Hydrophobic R Groups | TestYourSelf Answer Question 3

This KZbin short is a question about Polar R Groups in Aqueous Solutions. It's part of a TestYourSelf KZbin Shorts series run by The MCAT Tutor to help students with active recall and on-the-spot problem-solving. This series helps you study by giving MCAT multiple-choice questions while students scroll on social media.
This video explains why polar and nonpolar R groups play crucial roles in the structure and function of proteins. In an aqueous (water-based) environment, such as the cellular milieu, the behavior of these R groups is influenced by their hydrophilic or hydrophobic nature. Polar R groups contain electronegative atoms (e.g., oxygen or nitrogen), making them capable of forming hydrogen bonds with water molecules. These groups have an affinity for water. In proteins, polar R groups are often found on the surface, where they can interact with surrounding water molecules. This helps in maintaining the solubility of the protein in the aqueous environment of the cell. Polar R groups on the protein surface may be involved in interactions with other polar molecules, such as substrates or other proteins. They can participate in hydrogen bonding with water and contribute to the overall stability and structure of the protein. Nonpolar R groups lack significant electronegative atoms and are considered hydrophobic. They do not form favorable interactions with water. In contrast to polar R groups, nonpolar R groups tend to be buried within the interior of the protein. This behavior is driven by the desire to minimize contact with water, as water disrupts the cohesive interactions between nonpolar groups. The burial of hydrophobic regions within the protein's core is a key factor in protein folding. This hydrophobic effect contributes to the overall stability of the protein structure, as it minimizes the unfavorable interactions between nonpolar groups and water.
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