Retention of nativelike conformation by proteins embedded in high external electric fields.

Autor: Pompa, P. P., Bramanti, A., Maruccio, G., Cingolani, R., de Rienzo, F., Corni, S., di Felice, R., Rinaldi, R.
Předmět:
Zdroj: Journal of Chemical Physics; 5/8/2005, Vol. 122 Issue 18, p181102, 4p, 1 Diagram, 3 Graphs
Abstrakt: In this Communication, we show that proteins embedded in high external electric fields are capable of retaining a nativelike fold pattern. We have tested the metalloprotein azurin, immobilized onto SiO2 substrates in air with proper electrode configuration, by applying static fields up to 106–107 V/m. The effects on the conformational properties of protein molecules have been determined by means of intrinsic fluorescence measurements. Experimental results indicate that no significant field-induced conformational alteration occurs. Such results are also discussed and supported by theoretical predictions of the inner protein fields. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index