With the advancement in proteomics and bioinformatics, it is paramount to predict the
causes of aggregation in all Human Hydrolase Enzymes (HHE), which have more tendencies to
aggregate. Protein aggregation is associated with manifold pathological and neurodegenerative
diseases because of amyloid fibrillation. Physico-chemical factors responsible for aggregation were
studied in details. The positional dependencies of amylogenic regions in active participation for
aggregation in HHE were correlated and brought into limelight through this study. Novel deductions
from several studies in this research revealed that helical regions in the N-Terminal amylogenic
regions mainly contributed for aggregation in HHE, especially for the ones having acidic theoretical pI. The presence of
aggregation-prone highly fluctuating amino acid residues mainly in N-Terminal amylogenic regions was also explored.
Withal, mutational alterations in the active sites, that could reduce net aggregation propensity and free energy of folding
of entire HHE family leading to better foldability and reduction in the chances for the neurodegenerative disorders to be
caused were also discerned with supportive statistical significance.
Keywords: Amylogenic regions, free energy of folding, folding rate, mutational alteration, protein aggregation.
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