In this paper we report a procedure to analyze protein homodimer interfaces. We approached the problem by means of a topological methodology. In particular, we analyzed the subunits interface of about 50 homodimers and we have defined a few parameters that allow to organize these proteins in six different classes. The main characteristics of each class of homodimers have been discussed also taking into account their stabilization energy, as reported in the literature from the experimental measurements. A paradigmatic example for each class has been reported and a graphical representation proposed in order to better explain the meaning of the parameters chosen.
Mei, G., Di Venere, A., Di Paola, L., Finazzi Agro, A. (2021). Protein Assembly: Defining the Strength of Protein-Protein Interactions Coupling the Theory with Experiments. In Methods in Molecular Biology (pp. 77-88). Humana Press Inc. [10.1007/978-1-0716-1154-8_6].
Protein Assembly: Defining the Strength of Protein-Protein Interactions Coupling the Theory with Experiments
Mei G.;Di Venere A.;
2021-01-01
Abstract
In this paper we report a procedure to analyze protein homodimer interfaces. We approached the problem by means of a topological methodology. In particular, we analyzed the subunits interface of about 50 homodimers and we have defined a few parameters that allow to organize these proteins in six different classes. The main characteristics of each class of homodimers have been discussed also taking into account their stabilization energy, as reported in the literature from the experimental measurements. A paradigmatic example for each class has been reported and a graphical representation proposed in order to better explain the meaning of the parameters chosen.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
