On the role of aggregation prone regions in protein evolution, stability, and enzymatic catalysis: insights from diverse analyses.

ABSTRACT: The various roles that aggregation prone regions (APRs) are capable of playing in proteins are investigated here via comprehensive analyses of multiple non-redundant datasets containing randomly generated amino acid sequences, monomeric proteins, intrinsically disordered proteins (IDPs) and catalytic residues. Results from this study indicate that the aggregation propensities of monomeric protein sequences have been minimized compared to random sequences with uniform and natural amino acid compositions, as observed by a lower average aggregation propensity and fewer APRs that are shorter in length and more often punctuated by gate-keeper residues. However, evidence for evolutionary selective pressure to disrupt these sequence regions among homologous proteins is inconsistent. APRs are less

SUBMITTER: Buck PM 

PROVIDER: S-EPMC3798281 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature