Abstract.
Binding-energy landscapes are used to investigate the thermodynamics of molecular recognition for the pteridine ring, a recognition anchor in binding with dihydrofolate reductase, and two molecules with the same shape but different heteroatom substitutions. The relative importance of hydrogen bonding and hydrophobic interactions in this system is analyzed by comparing these three different decorations of the pteridine scaffold.
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Received: 5 May 1998 / Accepted: 3 September 1998 / Published online: 17 December 1998
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Rejto, P., Bouzida, D. & Verkhivker, G. Examining ligand-protein interactions with binding-energy landscapes. Theor Chem Acc 101, 138–142 (1999). https://doi.org/10.1007/s002140050420
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DOI: https://doi.org/10.1007/s002140050420