TY - JOUR
T1 - Thermodynamic features characterizing good and bad folding sequences obtained using a simplified off-lattice protein model
AU - Amatori, Andrea
AU - Ferkinghoff-Borg, Jesper
AU - Tiana, Guido
AU - Broglia, Ricardo A.
PY - 2006
Y1 - 2006
N2 - The thermodynamics of the small SH3 protein domain is studied by means of a simplified model where each
beadlike amino acid interacts with the others through a contact potential controlled by a 2020 random
matrix. Good folding sequences, characterized by a low native energy, display three main thermodynamical
ensembles, namely, a coil-like ensemble, an unfolded globule, and a folded ensemble plus two other states,
frozen and random coils, populated only at extreme temperatures. Interestingly, the unfolded globule has some
regions already structured. Poorly designed sequences, on the other hand, display a wide transition from the
random coil to a frozen state. The comparison with the analytic theory of heteropolymers is discussed
AB - The thermodynamics of the small SH3 protein domain is studied by means of a simplified model where each
beadlike amino acid interacts with the others through a contact potential controlled by a 2020 random
matrix. Good folding sequences, characterized by a low native energy, display three main thermodynamical
ensembles, namely, a coil-like ensemble, an unfolded globule, and a folded ensemble plus two other states,
frozen and random coils, populated only at extreme temperatures. Interestingly, the unfolded globule has some
regions already structured. Poorly designed sequences, on the other hand, display a wide transition from the
random coil to a frozen state. The comparison with the analytic theory of heteropolymers is discussed
U2 - 10.1103/PhysRevE.73.061905
DO - 10.1103/PhysRevE.73.061905
M3 - Journal article
SN - 1063-651X
VL - 73
JO - Physical Review E. Statistical, Nonlinear, and Soft Matter Physics
JF - Physical Review E. Statistical, Nonlinear, and Soft Matter Physics
ER -