Research article
The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: Understanding the determinants of binding affinity by comparison with Abl-SH3
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* Corresponding author: Nico AJ van Nuland najvan@ugr.es
- † Equal contributors
1 Departamento de Química Física e Instituto de Biotecnología, Facultad de Ciencias, Universidad de Granada, Campus Fuentenueva s/n, 18071 Granada, Spain
2 Bijvoet Center, Department of NMR Spectroscopy, Utrecht University, Padualaan 8, 3584CH Utrecht, The Netherlands
BMC Structural Biology 2007, 7:22 doi:10.1186/1472-6807-7-22
Published: 2 April 2007Additional files
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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