The interiors of globular proteins tend to be enriched for ______________ aminoacids while the protein surface regions near the aqueous environment tend to be _________________________

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Question restatement: The interiors of globular proteins tend to be enriched for ______________ aminoacids while the protein surface regions near the aqueous environment tend to be _________________________

Option 1: hydrophilic aminoacids, hydrophobic. This pairing would imply interiors are rich in hydrophilic residues and surfaces are hydrophobic, which contradicts the general tendency of hydrophobic residues to be buried away from water and hydrophilic residues to be solvent-exposed.

Option 2: negatively charged aminoacids, aromatic. While some surfaces can have charged residues, and some interiors may contain a few aromatics, this combination does not capture the dominant hydrophobic exclusion from water in core regions, nor a broad hydrophilic exterior pattern. The common core is not simply characterized by negative charges, and aromatics can appear both in core and surface, making this option unlikely as a general rule.

Option 3: hydrophobic aminoacids, hydrophilic. This aligns with the widely taught principle: globular protein cores are packed with hydrophobic amino acids to minimize unfavorable interactions with water, while the exterior near the aqueous environment is enriched in hydrophilic (often polar or charged) residues to interact favorably with water.

Option 4: positively charged aminoacids, hydrophobic. While positively charged residues exist on protein surfaces to engage in solvent interactions and salt bridges, labeling the entire surface as hydrophobic is inaccurate. Moreover, interiors are unlikely to be dominated by positively charged residues, which would be energetically costly in the hydrophobic core.

Synthesis: The widely observed pattern in globular proteins is a hydrophobic core and a hydrophilic, water-facing surface. Therefore, the choice that states interiors are rich in hydrophobic aminoacids and surfaces are rich in hydrophilic aminoacids best matches fundamental protein chemistry concepts. The other options either invert the polarity (surface hydrophobic, interior hydrophilic), rely on specific subcategories (negatively charged or positively charged and aromatic) without addressing the core-surface dichotomy, or propose an inconsistent generalization about core composition.

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The interiors of globular proteins tend to be enriched for aminoacids while the protein surface regions near the aqueous environment tend to be ___________

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