STUDY OF THE THERMAL STABILITY OF BARNASE PROTEIN MUTANTS WITH MOLKERN SOFTWARE

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 dramati...

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Bibliographic Details
Published in:Вавиловский журнал генетики и селекции
Main Authors: E. S. Fomin, N. A. Alemasov
Format: Article
Language:English
Published: Siberian Branch of the Russian Academy of Sciences, Federal Research Center Institute of Cytology and Genetics, The Vavilov Society of Geneticists and Breeders 2014-12-01
Subjects:
barnase
molecular dynamics
λ dynamics
free energy difference
protein thermal stability
Online Access:https://vavilov.elpub.ru/jour/article/view/57
Description
Summary: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.
ISSN:2500-3259

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