Autor: |
Pompa, P. P., Bramanti, A., Maruccio, G., Cingolani, R., de Rienzo, F., Corni, S., di Felice, R., Rinaldi, R. |
Předmět: |
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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 |
Externí odkaz: |
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