Artículo de revista
Effect of mutation at the interface of Trp-repressor dimeric protein: a steered molecular dynamics simulation
Fecha
2013Registro en:
Eur Biophys J (2013) 42:683–690
DOI 10.1007/s00249-013-0918-9
Autor
Miño Galaz, Germán
Báez, Mauricio
Gutiérrez Gallardo, Gonzalo
Institución
Resumen
The strength of key interfacial contacts that
stabilize protein–protein interactions have been studied by
computer simulation. Experimentally, changes in the
interface are evaluated by generating specific mutations at
one or more points of the protein structure. Here, such an
evaluation is performed by means of steered molecular
dynamics and use of a dimeric model of tryptophan
repressor and in-silico mutants as a test case. Analysis of
four particular cases shows that, in principle, it is possible
to distinguish between wild-type and mutant forms by
examination of the total energy and force–extension profiles.
In particular, detailed atomic level structural analysis
indicates that specific mutations at the interface of the
dimeric model (positions 19 and 39) alter interactions that
appear in the wild-type form of tryptophan repressor,
reducing the energy and force required to separate both
subunits.