Answer:
Option D
Step-by-step explanation:
If an aspartic acid were present in the interior of a globular protein, it would most likely change the conformation of the protein, maybe changing its shape and ultimately its function. To ensure compactness of the interior, hydrophobic amino acid are mainly found in the interior of globular proteins. This acid can be deprotonated and become negatively charged if the surrounding solution's pH is raised changing their isoelectric points.