Role of Solute Solvent Interactions of Aromatic Residues in Protein Folding Stability and Misfolding Mechanisms
Abstract: Aromatic amino acids tryptophan, tyrosine, and phenylalanine are consistently overrepresented in protein folding nuclei, hydrophobic cores, and oligomerization interfaces, reflecting the unusually favorable and versatile non-covalent interactions their ring systems support. This paper examines how solute solvent interactions of aromatic residues govern not only the stability of the correctly folded state but also the pathways by which proteins misfold and aggregate when solvent conditions are perturbed by chemical denaturants. We review the evidence that aromatic clusters frequently form the earliest, most persistent contacts during folding, discuss how partial or asymmetric denaturant exposure of these clusters generates on-pathway and off pathway intermediates, and examine the specific role of aromatic ?-stacking in amyloid and amorphous aggregation. We conclude with a discussion of osmolyte based protective strategies that counteract denaturant driven aromatic desolvation, linking mechanistic understanding to practical approaches for protein stabilization.
Keywords: Protein folding nucleus, molten globule, amyloid aggregation, π-stacking, osmolytes, misfolding
How to Cite?: Naseem Ahmed, "Role of Solute Solvent Interactions of Aromatic Residues in Protein Folding Stability and Misfolding Mechanisms", Volume 6 Issue 10, October 2017, International Journal of Science and Research (IJSR), Pages: 2185-2189, https://www.ijsr.net/getabstract.php?paperid=SR171004090525, DOI: https://dx.doi.org/10.21275/SR171004090525