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Mutations in proteins introduce structural
changes and influence biological activity: the specific
effects depend on the location of the mutation. The simple
method proposed in the present paper is based on a two-
step model of in silico protein folding. The structure of the
first intermediate is assumed to be determined solely by
backbone conformation. The structure of the second one is
assumed to be determined by the presence of a hydrophobic
center. The comparable structural analysis of the set of
mutants is performed to id
entify the mutant-induced
structural changes. The changes of the hydrophobic core
organization measured by the divergence entropy allows
quantitative comparison estimating the relative structural
changes upon mutation. The set of antifreeze proteins,
which appeared to represent the hydrophobic core structure accordant with
“
fuzzy oil drop
”
model was selected for
analysi
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