HYDE [1] is a function originally derived to score protein-ligand complexes. Due to its atomistic nature (embedding atomic logP increments) and owing to simple, yet sound, underlying physical principles, HYDE has emerged as a more generally applicable function for an elucidating assessment of interaction energies. Considering that no training to protein-ligand or protein-protein complexes has been involved, it occurs naturally that HYDE should have distinct advantages over the more traditional forcefield approaches, notably its unbiased view life science physics, especially when influenced by water.The importance of individual amino acids in a protein-protein interface becomes visible when HYDE scoring is applied. HYDE results will be compared to the experimental  'Ala scanning' hot spot assessments [2] on protein interfaces of hormone receptors with their bound peptide hormones.[1] Reulecke et al.  Chem Med Chem 2008 , 3(6):885-897; http://www.biosolveit.de/Hyde[2] Clackson, T., Wells, J. A. Science 1995,  267, 383-6.

General applicability of HYDE scoring: Applications to protein-protein interactions

244th National Meeting (2012)

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