title: Electric field effects on insulin chain-B conformation.
abstract: The response of proteins to different forms of stress continues to be a topic of major interest, especially with the proliferation of electromagnetic devices conjectured to have detrimental effects on human health. In this paper, we have performed molecular dynamics simulations on insulin chain-B under the influence of both static and oscillating electric fields, ranging from 10(7) to 10(9) V/m. We have found that both variants have an effect on the normal behavior of the protein, with oscillating fields being more disruptive to the structure as compared to static fields of similar effective strength. The application of a static field had a stabilizing effect on the secondary structure, restricting the inherent flexibility that is crucial for insulin's biological activity.
authors.affiliation: Applied Physics, School of Applied Sciences, RMIT University, GPO Box 2476V, Melbourne, Victoria, 3001, Australia.
authors.forename: Akin
authors.initials: A
authors.lastname: Budi
authors.forename: F Sue
authors.initials: FS
authors.lastname: Legge
authors.forename: Herbert
authors.initials: H
authors.lastname: Treutlein
authors.forename: Irene
authors.initials: I
authors.lastname: Yarovsky
mesh_terms: D003198:Computer Simulation; D004574:Electromagnetic Fields; D007328:Insulin / Q000737:chemistry* / Q000528:radiation effects*; D011487:Protein Conformation / Q000528:radiation effects; D017433:Protein Structure, Secondary / Q000528:radiation effects; D055672:Static Electricity; D013997:Time Factors
chemical_list: D007328:Insulin