SCORPIO version 2.0

Structure-Calorimetry Of Reported Protein Interactions Online

• Home
• Browse proteins
• Browse ligands
• Browse ITC data
• Browse structures
• Browse citations

ITC

Browse

• ITC data
• Instruments
• Interaction types
• Buffers
• Comments
• Comment definitions
• ΔC_p

Browse ITC comments

ITC comment	ITC comment defintion
Altered change in enthalpy and entropy from further studies on protonation events during binding, see http://scorpio2-dev.biophysics.ismb.lon.ac.uk/citation/view/94.	GENERAL_COMMENT
Binding too tight to measure directly. Data obtained by competition ITC.	GENERAL_COMMENT
Entropy units reported should be J/mol/K	GENERAL_COMMENT
ITC binding curves at this high affinity become too steep for accurate fitting, and the estimation of contingent parameters isconsequently less reliable.	GENERAL_COMMENT
Number of titrations: 3.	GENERAL_COMMENT
Number of titrations: 13.	GENERAL_COMMENT
Number of titrations: 4.	GENERAL_COMMENT
Number of titrations: 11.	GENERAL_COMMENT
Number of titrations: 3. n was held equal to 1 during the curve-fitting process.	GENERAL_COMMENT
Only ΔH and n were fitting parameters for the obsereved reaction heat for d-biotin with Ka fixed at the litterature value of 2.5E13.	GENERAL_COMMENT
Displacement titration experiments. Concentration of acetylpepstatin in the titration cell was 200 micromolar.	GENERAL_COMMENT

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