Additional file 1.

Thermodynamic analysis of protein-ligand binding using differential scanning calorimetry and two tables: Table 1: Ambiguous interaction restraints (AIR) and intermolecular NOE-derived distance restraints. Table 2: Apparent amide hydrogen-deuterium exchange rate constants and apparent Gibbs energies for the R21A Spc-SH3 domain at pH* 3.0 and 27.1°C, in its free form and in the presence of a 96% saturating concentration of the p41 peptide. description and equations used for analysis of DSC thermograms and list of AIR and SH3:P41 intermolecular NOEs and a list of amide hydrogen-deuterium exchange rate constants and apparent Gibbs energies.

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Casares et al. BMC Structural Biology 2007 7:22   doi:10.1186/1472-6807-7-22