Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
 

Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.

Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.

Chem Biol Drug Des. 2011 Jan 14;

Authors: Chandra K, Mustafi SM, Muthukumar S, Chary KV

The study of protein-ligand interaction has been of a great interest in contemporary structural biology. The understanding of the nature of such interaction and determining the associated binding affinities are of utmost importance. NMR has become a powerful tool in deriving information related to such interactions in proteins. NMR data provides the site-specific information even in the case of proteins having multiple-binding sites and populations of respective species. In this communication, we set out to use such information to derive the associated microscopic binding constants.

PMID: 21235730 [PubMed - as supplied by publisher]



Source: PubMed