INVESTIGADORES
FIDELIO Gerardo Daniel
congresos y reuniones científicas
Título:
Thermodynamic model for the study the multi step dissociation of an oligomeric protein coupled to unfolding equilibrium
Autor/es:
BURGOS I.,; DASSIE, S.A.; FIDELIO. G.D.
Lugar:
SALTA
Reunión:
Congreso; Latin American Protein Society Meeting and XXXIX Argentinean Biophysical Society (SAB); 2010
Institución organizadora:
Latin American Protein Society Meeting and XXXIX Argentinean Biophysical Society (SAB)
Resumen:
The use of thermodynamic
models has been of great importance for the study of folding-unfolding process
of proteins, including the effect of ligands and protein-protein interaction on
the stability of the native folded state (N).
In the present work we propose the formalism based on thermodynamics
equilibrium which describes an oligomeric protein (Nn) of n subunits
that is in equilibrium with the dissociated native monomer N and its unfolded state D throughout the respective sequential intermediate n-i states (oligomeric conformers where i=0,2, 4,
n), according to the scheme (a). Defining the relative partition
function for the protein system we attained the analytical expression of the
enthalpy relative to the reference state. The heat capacity can be obtained by
derivative of the enthalpy with respect to the temperature. We study the
evolution of the system given in (a)
by simulating different experimental conditions and thermodynamic parameters.
The developed model offers a solid tool to characterize complex calorimetric
thermogram profiles with the contribution and identification of each species in
the system.