We investigate how fundamental physicochemical properties and sequence composition shape the organization of proteins and proteomes. In particular, we explore the relationship between isoelectric point (pI), molecular weight (MW), amino-acid composition, cellular localization and biological function, and how these patterns are conserved across evolution.

Proteome-wide analyses reveal a highly non-random organization of protein pI–MW space, including a recurrent depletion of proteins around neutral pI. Understanding which features emerge from protein chemistry and which reflect additional functional or evolutionary constraints may provide new insights into the principles governing proteome organization.

Molecular weight–isoelectric point landscape of the human reference proteome. Protein sequences from UniProt; MW and pI calculated from sequence.

Current direction: extending these analyses across thousands of public reference proteomes to investigate the evolutionary conservation and mechanistic basis of protein physicochemical organization.