Retention of nativelike conformation by proteins embedded in high external electric fields.
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 10(6)-10(7) Vm. 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.
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National Nanotechnology Laboratories of INFM, University of Lecce, Via per Arnesano 73100 Lecce, Italy.
Bramanti
A
A
Maruccio
G
G
Cingolani
R
R
De Rienzo
F
F
Corni
S
S
Di Felice
R
R
Rinaldi
R
R