  We use LINUS, a procedure developed by Srinivasan and Rose, to provide a
physical interpretation of and to predict the secondary structures of proteins.
The secondary structure type at a given site is identified by the largest
conformational bias during short time simulations. We examine the rate of
successful prediction as a function of temperature and the interaction window.
At high temperatures, there is a large propensity for the establishment of
$\beta$-strands whereas $\alpha$-helices appear only when the temperature is
lower than a certain threshold value. It is found that there exists an optimal
temperature at which the correct secondary structures are predicted most
accurately. We find that this temperature is close to the peak temperature of
the specific heat. Changing the interaction window or carrying out longer
simulations approaching equilibrium lead to little change in the optimal
success rate. Our findings are in accord with the observation by Srinivasan and
Rose that the secondary structures are mainly determined by local interactions
and they appear in the early stage of folding.
