Author: Justina Jankauskaite; Brian Jiménez-García; Justas Dapkunas; Juan Fernández-Recio; Iain H. Moal
Title: SKEMPI 2.0: An updated benchmark of changes in protein-protein binding energy, kinetics and thermodynamics upon mutation Document date: 2018_6_7
ID: d0eynz67_16
Snippet: The entries also vary in the degree of structural order. While most correspond to interactions between folded domains, the database contains entries in which structuring occurs upon binding, such as protein-peptide interactions and, in the extreme case, the ACTR/NCBD interaction in which both binding partners become ordered upon binding [32] . Indeed, the requirements of having a structure in order to be included in the data set, ipso facto biase.....
Document: The entries also vary in the degree of structural order. While most correspond to interactions between folded domains, the database contains entries in which structuring occurs upon binding, such as protein-peptide interactions and, in the extreme case, the ACTR/NCBD interaction in which both binding partners become ordered upon binding [32] . Indeed, the requirements of having a structure in order to be included in the data set, ipso facto biases the data, and means that there is no representation of "fuzzy" complexes in which a diffuse structural ensemble in the bound state prevents the formation of a resolvable crystal.
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