Further Analysis of RTHα(N359Y)

In the previous post, I addressed the ab initio folding of thyroid hormone receptor alpha and its mutant variance, RTHα through a in silico protein folding program. Today, I address the potential interactions and stability of this receptors. The fundamental challenge of of protein analysis is the complexity of its residue-residue interactions. Since the protein structure is not fully resolved, except for the Ligand Binding Domain, the initial problem was figuring out a method by which its primary sequences could be folded. This issue was resolved through an ab initio folding of the protein, which means that the folding is not dependent on the homology structures. Therefore, this type of folding does not require the use of homology structures. In a past paper addressing the stability of the Aldose Reductase, Balendiran et al utilized the B-Factor parameter to analyze the relative stability selected domains. Using this method, I grouped the amino acid sequence according to each domain and analyzed the relative stability of each domain.

As aspected, the DNA-Binding and Hinge Domain is relatively destabilized in agreement with what was found in silico. However, the nuclear localization sequence (NLS-1) was demonstrated no significant perturbations compared to the wild type. Thus, I would not expect the localization pattern to differ from the wild-type.


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