Breaking the Protein Amino Acid Code (aka the Code of Life)

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• J. C. Phillips, Rutgers
• Friday 16 May 2008, 15:30-16:30
• TCM Seminar Room, Cavendish Laboratory.

If you have a question about this talk, please contact Mike Payne.

Note unusual time

Monolayer water films mediate interactions between proteins that determine protein functionality. Conventional molecular dynamics simulations view protein-water interactions in terms of “flickering” hydrogen bonds, parameterized by classical force fields with multiple adjustable parameters adjusted to fit dry crystallized protein structures. Following Pauling (and his pioneering electronegativity scale) and myself (the exact dielectric ionicity scale for semiconductors), I examine several universal hydrophobicity scales, and identify the best one, which appears also to be exact!. With this scale one can recognize phantom water-protein interactions that are invisible to conventional analysis, and analyze protein functionality, as illustrated by several examples of proteins containing 300-900+ amino acid side groups. The success of this scale confirms an attractive conjecture, that proteins have evolved to be self-organized critical ensembles.

This talk is part of the Irregular seminars in TCM series.

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