Abstract

π–π Interactions play an important role in the stability of protein structures. In the present study, we have analyzed the influence of π–π interactions in eNOS and nNOS proteins. The contribution of these π–π interacting residues in sequential separation, secondary structure involvement, solvent accessibility and stabilization centers has been evaluated. π–π interactions stabilize the core regions within eNOS and nNOS proteins. π–π interacting residues are evolutionary conserved. There is a significant number of π–π interactions in spite of the lesser natural occurrences of π-residues in eNOS and nNOS proteins. In addition to π–π interactions, π residues also form π–π networks in both eNOS and nNOS proteins which might play an important role in the structural stability of these protein structures.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call