Dear Colleagues,

Most of the proteins and enzymes that govern the life of cells exist as oligomers, suggesting that forming supramolecular aggregates provide important evolutionary advantages. Multisubunit proteins play a key role in the main metabolic pathways, speeding up reactions and exerting fine-tuned control of the complex biochemical processes that take place in all living organisms. Such tasks are accomplished through tight cooperation among monomers, which give rise to new structural and functional properties, which are unachievable in a single chain protein. Another explanation for the widespread presence of oligomers in nature comes from thermodynamic studies. Kinetic and equilibrium folding/unfolding measurements have, in fact, demonstrated that the quaternary structure generally increases single monomers’ stability, being very often the main driving force of their folding pathway. On the other hand, several kinds of network analysis have demonstrated how local perturbation in one subunit can be transmitted to the others through a few contacts localized at the interface(s) that separate them, thus inducing researchers of different fields to focus their interest on the structural characterization of such interfaces. Such a task is important, not only to better understand the structural and functional properties of these macromolecules but also because it may shed new light on the more general protein–protein interaction process, a physical event that fundamentally encompasses most human body physiological features, including muscles contraction, signal transmission, and molecular recognition, to mention a few. Despite the structural and functional advantages provided by multisubunit assembly and cooperation, in some cases monomers association might yield wrong folded intermediates that can lead to aggregation and severe pathologies. 

This Special Issue, “Structural, Functional, and Folding Strategies of Oligomeric Proteins” will collect papers in this research field dealing with one of the following topics: a) folding pathways in multisubunit proteins; b) cooperative effects in multimeric structures; c) structural features of intersubunit interfaces; d) contact networks and symmetry analysis of oligomers; and e) the wrong face of oligomerization: aggregation and disease.

Prof. Giampiero Mei
Dr. Luisa Di Paola
Guest Editors

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• oligomers folding
• protein contact network
• protein aggregation
• oligomers hierarchy
• misfolding
• protein–protein interface