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. Author manuscript; available in PMC: 2010 May 15.
Published in final edited form as: Proteins. 2009 May 15;75(3):556–568. doi: 10.1002/prot.22271

Table 1.

DSC data for inhibitor binding to PR, PRD25N and PRD29N

Inhibitor Tm (°C) ΔTm (°C) KL at Tm (μM)a KL at 25 °C (nM)

PR PRD25N PRD29N PR PRD25N PRD29N PR PRD25N PRD29N PR
(lit.)
PR
(calc.)a

none 65.7 58.4 59.0 - - - - - - - -
DRV 88.1 61.5 72.7 22.4 3.1 13.7 0.018 16.6 1.34 0.005b;
0.010c
0.014
ATV 86.5 61.4 71.7 20.8 3.0 12.7 0.036 17.4 1.80 0.035 c 0.186
SQV 85.0 62.6 72.3 19.3 4.2 13.3 0.066 10.0 1.51 0.28d,e 8.14
RTV 81.3 61.1 66.1 15.6 2.7 7.1 0.27 20.5 9.3 0.10d,e 9.72
APV 80.0 58.7 67.5 14.3 0.3 8.5 0.44 274 6.2 0.2d,e 3.46
DMP323 81.0 67.3 69.2 14.7 8.9 10.2 0.30 1.6 3.7 3.8 f -
RPB 74.4 64.6 59.2 8.7 6.2 0.2 2.9 4.4 1178 50 g -
Ac-PEP 72.2 58.8 58.3 6.5 0.4 - 6.1 202 - 440 e 2956
a

Ligand dissociation constants calculated by the method of Brandts and Lin27 with ΔH = 43.3, 53.1 and 26.4 kcal/mol (this work) for PR, PRD25N and PRD29N, respectively. ΔCP = 3 kcal/mol·degree as measured25,26 for PR was used in calculations for all three constructs. KL values for PR at Tm (this work) and at 25 °C are italicized for ease of comparison.

Cited from Refs.

b

12

c

39

d

26

e

40

f

38

g

17