Energetic innovation across the tree of life
The thermodynamic atlas of proteomes is a computational biology resource consisting of residue-by-residue thermodynamic annotation of over 10,000 distinct proteomes, collectively representing each domain of life.
Download the database
Download thermodynamic environment annotation files covering bacterial, archaeal, and eukaryotic proteomes. The organisms represented are drawn from the Uniprot reference proteomes.
Cite the database
The peer-reviewed manuscript accompanying this database is published in "Molecular Biology and Evolution" under the title "A thermodynamic atlas of proteomes reveals energetic innovation across the tree of life."
About the database
Thermodynamic annotation was achieved by application of the eScape algorithm , which labels a protein's primary sequence with a series of thermodynamic environment (TE) labels. Each thermodynamic environment corresponds to a specific combination of average stability (free energy), enthalpy (with polar and apolar contributions), and conformational entropy, all with respect to individual amino acid resides in a protein. The TE energetic representation of a protein is explicitly not equivalent with a structural description of a protein.
The Hilser Lab
This database was created by and is maintained by the Hilser Lab in the Department of Biology at Johns Hopkins University.