RESUMO
Simple symmetry considerations would suggest that the transition from the smectic-A phase to the long-range bond-orientationally ordered hexatic smectic-B phase should belong to the XY universality class. However, a number of experimental studies have reported over the past twenty years "novel" critical behavior with non-XY critical exponents for this transition. Bruinsma and Aeppli argued [Phys. Rev. Lett. 48, 1625 (1982)], using a 4-epsilon renormalization-group calculation, that short-range molecular herringbone correlations coupled to the hexatic ordering drive this transition first order via thermal fluctuations, and that the critical behavior observed in real systems is controlled by a "nearby" tricritical point. We have revisited the model of Bruinsma and Aeppli and present here the results of our study. We have found two nontrivial strongly coupled herringbone-hexatic fixed points apparently missed by these authors. Yet, these two nontrivial fixed points are unstable, and we obtain the same final conclusion as the one reached by Bruinsma and Aeppli, namely that of a fluctuation-driven first-order transition. We also discuss the effect of local twofold distortion of the bond order as a possible "extra" order parameter in the Hamiltonian.
RESUMO
The Monte Carlo technique is used to simulate the energy landscape and the folding kinetics of a minimal prion-like protein model. We show that the competition between hydrogen-bonding and hydrophobic interactions yields two energetically favored secondary structures, an alpha-helix and a beta-hairpin. Folding simulations indicate that the probability of reaching the alpha-helix form from a denatured random conformation is much higher than the probability of reaching the beta-sheet form, even though the beta-sheet has a lower energy. The existence of a lower energy beta-sheet state gives the possibility for the normal alpha-helix structure to take a structural transformation into the beta-sheet structure under external influences.
Assuntos
Modelos Químicos , Príons/química , Dobramento de Proteína , Ligação de Hidrogênio , Cinética , Método de Monte Carlo , Conformação Proteica , Estrutura Secundária de Proteína , TermodinâmicaRESUMO
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.