STUDY OF THE THERMAL STABILITY OF BARNASE PROTEIN MUTANTS WITH MOLKERN SOFTWARE
Abstract
A thermal stability study of several barnase mutants has been carried out by the λ dynamics method. The method has been implemented in the MOLKERN software package. Mutations of amino acids with non-zero charge are chosen for the study, because in this case λ dynamics gives results differing dramatically (> 10 kJ/mol) from experimental data in nearly one-fourth of cases. A new modification of λ potentials is proposed, which takes into account charge changes, as well as the Net-Q method, in order to obtain reliable charge distributions for charged amino acids. The results obtained for the R72G mutation show a better agreement with experimental values than the results of other authors.
About the Authors
E. S. Fomin
Institute of Cytology and Genetics, SB RAS, Novosibirsk, Russia
Russian Federation
Russian Federation
N. A. Alemasov
Institute of Cytology and Genetics, SB RAS, Novosibirsk, Russia
Russian Federation
Russian Federation
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