NR AMQH
AU Wind,A.F.; Kemp,J.P.; Ermoshkin,A.V.; Chen,J.Z.
TI Structural and folding properties of a lattice prion model
QU Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics 2002 Sep; 66(3 Pt 1): 031909
PT journal article
AB Searching through and conducting Monte Carlo folding simulations on 10(6) different 27 mer sequences, we have selected a prionlike lattice model whose energy spectrum and folding properties demonstrate characteristic prion behavior. The energetic competition and structural partition between two closely spaced energy minima yield unique kinetic and thermodynamic properties that can be qualitatively compared with experimental results. Folding simulations indicate that the probability of reaching the first excited state from a denatured random conformation is much higher than the probability of reaching the global energy-minimum state.
MH Biophysics; Kinetics; Models, Molecular; Monte Carlo Method; Prions/*chemistry; Protein Binding; Protein Conformation; Protein Folding; Support, Non-U.S. Gov't; Thermodynamics; Time Factors
AD Department of Physics, University of Waterloo, Waterloo, Ontario, Canada N2L 3G1.
SP englisch
PO USA