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A comparative analysis of the stability of the chymotrypsin charge triad
Author(s) -
Shibata Masayuki,
KieberEmmons Thomas,
Dutta Shibani,
Rein Robert
Publication year - 1981
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.560200737
Subject(s) - ab initio , triad (sociology) , charge (physics) , chemistry , chymotrypsin , ionic bonding , chemical physics , stability (learning theory) , computational chemistry , physics , ion , quantum mechanics , enzyme , computer science , trypsin , organic chemistry , psychology , psychoanalysis , machine learning
The energetics of the α‐chymotrypsin charge triad, taking into account the interaction energies of the components of the charge relay system and its surrounding environment, have been calculated. These results are compared with corresponding ab‐initio MO energies and thermodynamic values as taken from the literature. The following conclusions can be drawn from this analysis. The ab‐initio and interaction calculations yield results which are in good agreement, suggesting that the latter, while computationally easy for implementations, is reliably good for the study of large systems such as enzymes. The theoretical prediction for the most stable state of the charge relay system depends upon the model assumed for the environment. In keeping with available crystallographic data, and thereby allowing for partial hydration of the serine residue, the zwitter ionic state is found to be the most stable.