Predicting changes in protein thermostability brought about by single- or multi-site mutations

BMC Bioinformatics

Table 2 Structural features used in Prethermut

Feature	Program^a	Feature	Program
Total energy	FoldX	Stereochemical improper dihedral potential	Modeller 9.7
Backbone H-bond	FoldX	Frequency_[0,2.1) ^b	Modeller 9.7
Sidechain H-bond	FoldX	Frequency_[2.1,2.2)	Modeller 9.7
Van der Waals forces	FoldX	Frequency_[2.2,2.3)	Modeller 9.7
Electrostatic attractions	FoldX	Frequency_[2.3,2.4)	Modeller 9.7
Solvation polar	FoldX	Frequency_[2.4,2.5)	Modeller 9.7
Solvation hydrophobic	FoldX	Frequency_[2.5,2.6)	Modeller 9.7
Van der Waals clashes	FoldX	Frequency_[2.6,2.7)	Modeller 9.7
Entropy side chain	FoldX	Frequency_[2.7,2.8)	Modeller 9.7
Entropy main chain	FoldX	Frequency_[2.8,2.9)	Modeller 9.7
Torsional clash	FoldX	Frequency_[2.9,3.0)	Modeller 9.7
Backbone clash	FoldX	Frequency_[3.0,3.1)	Modeller 9.7
Helix dipole	FoldX	Frequency_[3.1,3.2)	Modeller 9.7
Current energy	Modeller 9.7	Frequency_[3.2,3.3)	Modeller 9.7
Bond energy	Modeller 9.7

^aThe corresponding feature was calculated by the programs (FoldX [11, 28] and Modeller 9.7 [29]). ^bThe frequency of short non-covalent contacts with a distance of less than 2.1 Å.

ISSN: 1471-2105