Fundamentals of Thermodynamics by Claus Borgnakke, Richard E. Sonntag

By Claus Borgnakke, Richard E. Sonntag

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It follows that the dielectric constant of ei = 20 derived from the lysozyme pK,’s is likely to be an upper bound to the effective dielectric constant of the protein in the context of titration calculations with a single protein conformer. Thus, we use ei = 20 rather than a larger effective dielectric constant, despite the fact that ei > 20 gives similar results in the case of lysozyme. The finding that protein relaxation due to changes in the ionization state corresponds to an effective dielectric constant of ei = 20 for the protein is consistent with the observation that the Tanford-Kirkwood model of protein titration (Tanford and Kirkwood, 1957) gives best agreement with experiment when the charges are placed at the surface of the protein sphere (with ei = 2 to 4),where the solvent screening of charge-charge interactions is significant even at short distances.

10 (and 38 MICHAEL SCHAEFER ET AL. for the folding energy of the standard charge state). It follows that it is the variation in the interactions of polar atom groups in the different lysozyme structures that accounts for the variation in the calculated absolute pH stability of lysozyme and that the interaction of titrating sites is comparatively independent of the choice for the native and unfolded structure. , hydrogen bonds), which are more sensitive to structural changes. 4. Conclusions We have used the linked function treatment of protein titration to calculate the titration curves of the crystal structure and an extended structure of lysozyme as models for the native and denatured state.

This results in 90, 88, and 90 titratable residues per protomer for types 0,A10, and A22, respectively. In the titration program of Beroza et al. (1991), 7500 Monte Carlo steps were performed to determine the average protonation of all sites at a given pH and the titration curves were calculated using 121 pH values evenly distributed in the interval from 0 to 12. , 1977). , 1996), and the empty capsid structure of A22 (called A22E), were provided by S. Curry, E. Fry, and D. 0 A resolution). 35 The protomers consist of 736, 736, and 737 residues, for OIBFS, A10, and A22, respectively.

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