Finding
Experimental results indicate that no significant field-induced conformational alteration occurs.
Paper
Retention of nativelike conformation by proteins embedded in high external electric fields.
Abstract
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.
Authors
P. Pompa, A. Bramanti, G. Maruccio
Journal
The Journal of chemical physics
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