The role of secondary structure in protein structure selection.

The presence of highly regular secondary structure motifs in protein structure is a fascinating area of study. The secondary structures play important roles in protein structure and protein folding. We investigate the folding properties of protein by introducing the effect of secondary structure elements.

Model study of prionlike folding behavior in aggregated proteins.

We investigate the folding behavior of protein sequences by numerically studying all sequences with a maximally compact lattice model through exhaustive enumeration. We get the prionlike behavior of protein folding. Individual proteins remaining stable in the isolated native state may change their conformations when they aggregate.

Medium effects on the selection of sequences folding into stable proteins in a simple model.

We study the medium effects on the selection of sequences in protein folding by taking into account surface potential in hydrophobic-polar model. Our numerical calculation demonstrates that the surface potential enhances the average gap for the highly designable structures. It also shows that the most stable structure may be no longer the most stable one if the medium is changed.

Role of chaos in one-dimensional heat conductivity.

We investigate the heat conduction in a quasi-one-dimensional gas model with various degrees of chaos. Our calculations indicate that the heat conductivity kappa is independent of system size when the chaos of the channel is strong enough. The different diffusion behaviors for the cases of chaotic and nonchaotic channels are also studied.