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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.