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- W2157593422 abstract "We welcome the ‘Research News’ article about our recent paper [ 1 Carter C.W. et al. Four-body potentials reveal protein-specific correlations to stability changes caused by hydrophobic core mutations. J. Mol. Biol. 2001; 311: 625-638 Crossref PubMed Scopus (103) Google Scholar ] establishing a connection between four-body database-derived likelihood potentials and experimental mutational free energy changes. The Delaunay tetrahedron is the simplest three-dimensional packing motif; we noted in our article, and presented more fully elsewhere [ 2 Cammer, S. et al. Identification of sequence-specific tertiary packing motifs in protein structures using Delaunay tessellation. In Lecture Notes in Computational Science and Engineering (Schlick, T., ed). Springer-Verlag, New York (in press) Google Scholar ] that, unlike potentials of smaller dimensionality, joint consideration of four interacting side chains achieves excellent proportionality between statistical and thermodynamic four-body potentials (calculated by summing the transfer free energies, or hydrophobicities, of the four interacting side chains). Decomposing tertiary structure into elementary three-dimensional simplices therefore appears to afford a decisive new coherence to side-chain packing analysis." @default.
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- W2157593422 date "2002-01-01" @default.
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- W2157593422 title "Energetics of enzyme stability: Response from Carter, Tropsha and Edgell" @default.
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- W2157593422 doi "https://doi.org/10.1016/s0167-7799(01)01872-8" @default.
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