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Calculation of the thermodynamic quantities of solvation for lysozyme and β-lactoglobulin a in guanidinium chloride

✍ Scribed by Savo Lapanje

Publisher
Wiley (John Wiley & Sons)
Year
1984
Tongue
English
Weight
430 KB
Volume
23
Category
Article
ISSN
0006-3525

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✦ Synopsis

The thermodynamic quantities of solvation, that is, Gibbs free energy, enthalpy, and entropy for the transfer of lysozyme and 0-lactoglobulin A from water to 6M guanidinium chloride solution, were calculated from the respective contributions of constituent groups. Comparison of the calculated values with the experimental ones reveals satisfactory agreement for lysozyme, whereas for P-lactoglobulin A, it is semiquantitative. Thus the method of calculation appears to be fundamentally sound. The reasons for the differences in calculated and experimental value are briefly discussed.

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Performance comparison of generalized born and Poisson methods in the calculation of electrostatic solvation energies for protein structures
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## Abstract This study compares generalized Born (GB) and Poisson (PB) methods for calculating electrostatic solvation energies of proteins. A large set of GB and PB implementations from our own laboratories as well as others is applied to a series of protein structure test sets for evaluating the