Topological change and impedance responses in proteins: How do they run together?
نویسندگان
چکیده
In recent experiments, the conformational change of proteins has been monitored by means of electrical measurements. In this paper we propose a model able to reproduce the variation of some conductive features of a protein resulting by its morphological transformations. To this purpose we map each protein into a network of interacting elementary impedances. The biological root (the kind of aminoacids and their mutual distance) determines the value of each elementary impedance. Accordingly, a global impedance is determined for each protein configuration. Thus, the value of the impedance is put in correspondence with the native or activated state of the protein. With this method we are also able to asses the size of the conformational change. The model is applied to the study of two quite different proteins, the light trans-membrane receptor, bovine rhodopsin, and the enzyme acetylcholinesterase (AChE). The results obtained for these proteins support the scenario in which conformational change is large in size and widespread in rhodopsin, while it is localized and small in AChE. PACS numbers: 87.15.A-,87.14.E-, 87.15.hp,87.80.Nj
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