Functionality is at the core of our understanding of biological systems, as inert physical systems lack this sense of function. Accounting for biological function thus requires a new kind of physics. Our group investigates biological functionaly by exploring new regimes of statistical physics, mechanics and thermodynamics. We are particularly interested in how nonequilibrium driving enables biological function, acting as an unavoidable cellular cost.
One fundamental characteristic of proteins is that they self-assemble into higher order structures. These structures can be solid (e.g. protein complexes such as the ribosome) or liquid (e.g. Cajal bodies). Self-assembly occurs in the cytoplasm, a mixture of thousands of different protein species. This makes accurate assembly a formidable discriminatory task, as each growing complex needs to distinguish its few constituent proteins. What are the states of matter of a mixture of thousands of proteins? Is self-assembly a robust phase? What are the generic properties of assemblies that allow them to self-assemble accurately?
The function of proteins is determined by the motion of its atomic structure. Different molecular forces underlay the motion of the large number of atoms in an protein. This makes the potential dimensionality of protein function formidably large. Surprisingly, very simple mechano-chemical descriptions of proteins, with two or three degrees of freedom, have been greatly succesful in biophysics. How do such simple descriptions emerge from the high dimensional structural description of proteins? Can we describe proteins as a “special” kind of evolved material?
Metabolic versatility enables unicellular organisms to grow in vastly different environments. Since growth occurs far from thermodynamic equilibrium, the second law of thermodynamics has long been believed to pose key constraints to life. What are the phenomenological rules relating microbial dissipation to their basic physiology? Can we derive such rules from first principles? What are their evolutionar implications?
Some selected publication from the last 3 years:
Cossetto T, Rodenfels J, Sartori P. Thermodynamic dissipation constrains metabolic versatility of unicellular growth. bioRxiv. 2024;2024.03.21.585772.
Benoist F, Sartori P. High-speed combinatorial self-assembly through kinetic-trap encoding. Phys Rev Lett. 2024;134:038402.
Braz Teixeira R, Carugno G, Neri I, Sartori P. Liquid Hopfield model: retrieval and localization in multicomponent liquid mixtures. Proc Natl Acad Sci U S A. 2024;121(48):e2320504121.
Sartori P, Leibler S. Evolutionary conservation of mechanical strain distributions in functional transitions of protein structures. Phys Rev X. 2024;14(1):011042.
Mello VH, Wald J, Marlovits TC, Sartori P. Elastic analysis of structural ensemble reveals the energetic basis of hand-over-hand in a AAA+ motor. bioRxiv. 2024;2024.10.04.616613.
Geyer VF, Howard J, Sartori P. Ciliary beating patterns map onto a low-dimensional behavioural space. Nat Phys. 2022;18(3):332–337.
A complete list of publications can be found here.
Mello VH, Wald J, Marlovits TC, Sartori P. Elastic analysis of structural ensemble reveals the energetic basis of hand-over-hand in a AAA+ motor. bioRxiv. 2024;2024.10.04.616613.
Geyer VF, Howard J, Sartori P. Ciliary beating patterns map onto a low-dimensional behavioural space. Nat Phys. 2022;18(3):332–337.
A complete list of publications can be found here.
Physical Review X: Outstanding reviewer award
Google Scholar: https://scholar.google.com/citations?hl=en&user=bWdwdRwAAAAJ