The electrical properties of a set of seven-helix transmembrane proteins, whose space arrangement [threedimensional (3D) structure] is known, are investigated by using regular arrays of the amino acids. These structures, specifically cubes, have topological features similar to those shown by the chosen proteins. The theoretical results showa good agreement between the predicted current-voltage characteristics obtained from a cubic array and those obtained from a detailed 3Dstructure. The agreement is confirmed by available experiments on bacteriorhodopsin. Furthermore, all the analyzed proteins are found to share the same critical behavior of the voltage-dependent conductance and of its variance. In particular, the cubic arrangement evidences a short plateau of the excess conductance and its variance at high voltages. The results of the present investigation show the possibility to predict the I -V characteristics of a multiple-protein sample even in the absence of detailed knowledge of the proteins’ 3D structure.
Current-voltage characteristics of seven-helix proteins from a cubic array of amino acids
ALFINITO, ELEONORA
2016-01-01
Abstract
The electrical properties of a set of seven-helix transmembrane proteins, whose space arrangement [threedimensional (3D) structure] is known, are investigated by using regular arrays of the amino acids. These structures, specifically cubes, have topological features similar to those shown by the chosen proteins. The theoretical results showa good agreement between the predicted current-voltage characteristics obtained from a cubic array and those obtained from a detailed 3Dstructure. The agreement is confirmed by available experiments on bacteriorhodopsin. Furthermore, all the analyzed proteins are found to share the same critical behavior of the voltage-dependent conductance and of its variance. In particular, the cubic arrangement evidences a short plateau of the excess conductance and its variance at high voltages. The results of the present investigation show the possibility to predict the I -V characteristics of a multiple-protein sample even in the absence of detailed knowledge of the proteins’ 3D structure.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
