**Core Concept**
The question tests the understanding of protein misfolding and its relation to human diseases, specifically focusing on conformational isomerization. Protein misfolding occurs when a protein does not fold into its native, functional conformation, leading to various disorders.

**Why the Correct Answer is Right**
Conformational isomerization refers to the process by which a protein changes its shape, often leading to misfolding. This misfolding can result in the protein aggregating and forming insoluble fibrils that are toxic to cells. One notable example of a disorder arising from conformational isomerization is **Prion Disease**, such as Creutzfeldt-Jakob disease, where the misfolded prion protein (PrP^Sc) induces normal prion proteins (PrP^C) to also misfold.

**Why Each Wrong Option is Incorrect**
**Option A:** This option is incorrect because while it may be related to protein dysfunction, it does not specifically result from conformational isomerization.
**Option B:** Similarly, this option does not directly relate to the consequences of conformational isomerization of proteins.
**Option C:** This option is also incorrect as it does not accurately represent a disorder caused by conformational isomerization.

**Clinical Pearl / High-Yield Fact**
A key point to remember is that protein misfolding diseases, including those caused by conformational isomerization, can lead to severe neurological disorders. Understanding the mechanisms behind these diseases is crucial for developing therapeutic strategies.

**Correct Answer:** D. Prion Disease.