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- W2583179924 abstract "The single-molecule enzyme-turnover-time histogram of cholesterol oxidase [1] resembles the blackbody radiation spectrum at 4000 °K. This observation motivated the author to generalize the Planck radiation equation (PRE), Sλ = (8πhc/λ5)/(ehc/λkT − 1), by replacing the universal constants and temperature by free parameters, resulting in the Planckian Distribution Equation (PDE), y = (A/(x + B)5)/(eC/(x + B) − 1) [2]. Since the first factor in PRE reflects the number of standing waves generated in the blackbody and the second factor the average energy of the standing waves [3], it was postulated that any material system that generates data fitting PDE can be interpreted as implicating standing waves with associated average energies [2]. PDE has been found to fit the long-tailed histogram of the folding free-energy changes measured from 4,300 proteins isolated from E. coli [4]. One possible interpretation of this finding is (i) that proteins (P) and their hydration shells (HS) are organized systems of oscillators with unique sets of natural frequencies, (ii) Ps assume their conformations whose standing waves are frequency-matched (or resonate) with the standing waves of their HSs, and (iii) the folding free energies are determined by the resonance frequencies of the P-HS complexes.[1] Lu, H. P., Xun, L. and Xie, X. S. (1998). Single-Molecule Enzymatic Dynamics. Science 282, 1877-1882.[2] Ji, S. (2012) Isomorphism between Blackbody Radiation and Enzyme Catalysis. In: Molecular Theory of the Living Cell: Concepts, Molecular Mechanisms and Biomedical Applications. Springer, New York, pp. 343-368. http://www.conformon.net/wp-content/uploads/2012/11/Isomorphism_blackbody_radiation_enzymic_catalysis_p343_p368.pdf[3] Blackbody radiation. http://hyperphysics.phy-astr.gsu.edu/hbase/mod6.html[4] Dill, K. A., Ghosh, K. and Schmidt, J. D. (2011) Physical limits of cells and proteomes. PNAS 108:17876-82." @default.
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- W2583179924 date "2017-02-01" @default.
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- W2583179924 title "Protein Folding as a Resonance Phenomenon, with Folding Free Energies Determined by Protein-Hydration Shell Interactions" @default.
- W2583179924 doi "https://doi.org/10.1016/j.bpj.2016.11.317" @default.
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