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Structure-Calorimetry Of Reported Protein Interactions Online

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ITC

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ITC datum

Protein and Ligand
Protein name	HIV-1 Protease
Ligand name	KNI-764 KNI-764
Interaction type	Synthetic ligands
ITC data	ITC data
Structure data	Structure data
ITC Information
n		±
ΔG	-62.34	±	kJ/mol
ΔH	-33.47	±	kJ/mol
-TΔS	28.87	±	kJ/mol
KD	0.0	± 0.0	uM
ΔCP		±
Notes on error determination	Not available
General comments	Displacement titration experiments. Concentration of acetylpepstatin in the titration cell was 200 micromolar.
Warnings	Affinity (0.0000) less than 0.0000. It is difficult to interpred ITC data if Affinity is less than 0.0000 as the sigmoidal curve becomes too sharp. This can be overcome by performing displacement experiments. DeltaG (-62.34) less than -60.00. It is difficult to interpred ITC data if DeltaG is less than -60.00 as the sigmoidal curve becomes too sharp. This can be overcome by performing displacement experiments.
Instrument	VP-ITC Microcalorimeter
Temp. (K)	298.15	pH	5.0
Buffer	DMSO 2.00 % Sodium Acetate 10.00 mM
Cell content	Protein
Reference	Biochemistry [2002] 41, 8613-8619

Disclaimer

This is an ongoing project and, although SCORPIO has been curated with great care, it may contain errors. If you spot an error please contact us. We take no responsibility for the data within SCORPIO, nor any responsibility for the consequences of using the data within SCORPIO. No contract, warranty or liability is implied by using the data within SCORPIO.

If you make use of SCORPIO please cite J. Mol. Biol. [2008] 384, 1002-1017
Tjelvar S. G. Olsson, Mark A. Williams, Will R. Pitt and John E. Ladbury