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Updated: Feb 7, 2026

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
Published on: March 17, 2010
SKEMPI 2.0: an updated benchmark of changes in protein-protein binding energy, kinetics and thermodynamics upon
Justina Jankauskaite1, Brian Jiménez-García2,3, Justas Dapkunas1
1Institute of Biotechnology, Life Sciences Center, Vilnius University, Vilnius, Lithuania.
Motivation:
Understanding the relationship between the sequence, structure, binding energy, binding kinetics and binding thermodynamics of protein-protein interactions is crucial to understanding cellular signaling, the assembly and regulation of molecular complexes, the mechanisms through which mutations lead to disease, and protein engineering.
Results:
We present SKEMPI 2.0, a major update to our database of binding free energy changes upon mutation for structurally resolved protein-protein interactions. This version now contains manually curated binding data for 7085 mutations, an increase of 133%, including changes in kinetics for 1844 mutations, enthalpy and entropy changes for 443 mutations, and 440 mutations, which abolish detectable binding.
Availability And Implementation:
The database is available as supplementary data and at https://life.bsc.es/pid/skempi2/.
Supplementary Information:
Supplementary data are available at Bioinformatics online.
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