SKEMPI 2.0: An updated benchmark of changes in protein-protein binding energy, kinetics and thermodynamics upon mutation
Preprint
- 7 June 2018
- preprint
- Published by Cold Spring Harbor Laboratory in bioRxiv
- p. 341735
- https://doi.org/10.1101/341735
Abstract
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: The database is available at https://life.bsc.es/pid/skempi2/Keywords
All Related Versions
- Published version: Bioinformatics, 35 (3), 462.
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