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Table 1 Results from the thermal shift assays on eight proteins, ranked by best ligand binding*

From: Experimental validation of FINDSITEcomb virtual ligand screening results for eight proteins yields novel nanomolar and micromolar binders

Protein

Organism

No. of ligands tested

No. of good curves

No. of + veashifts/% + veashifts

Best hit (NSC)

ΔTm(°C)

KD(nM)b

Best hit structure

DHFR

E. coli

83

32

15/46.9

309401

30.74

48.21

1000006

H. sapiens

59

43

6/13.9

133351

16.76

168.29

1000001

R. norvegicus

86

42

10/23.8

134137

12.30

406.0

TrpRS

H. sapiens

94

12

5/41.7

750690

14.57

1277.51

UCE

P. falciparum

80

51

2/03.9

93427

14.86

1376.09

TP2

P. falciparum

67

12

2/16.7

106231

5.7

40872.77

cDPK

H. sapiens

80

19

3/15.8

27032

2.95

48538.90

NAP 1

P. knowlesi

82

54

4/07.4

36398

2.21

180135.58

  1. 1000001: Carboxy-terminus phosphatase domain of protein tyrosine phosphatase (2NV5), DHFR: Dihydrofolate reductase, UCE: Ubiquitin conjugating enzyme, TrpRS: Tryptophanyl tRNA synthetase, TP2: Thioredoxin peroxidase 2, 1000006: catalytic domain of protein tyrosine phosphatase (2G59), cDPK: Catalytic subunit of cAMP-dependent protein kinase, NAP1: Nucleosome assembly protein 1. aPositive thermal shift is indicated by the notation + ve. KD indicates dissociation constants. bThe dissociation constant reported in this table are computed from the thermal shifts obtained. *The values reported in this table are experimental in-vitro values.