The Pepstr server predicts the tertiary structure of small peptides with sequence length varying between 7 to 25 residues. The prediction strategy is based on the realization that β-turn is an important and consistent feature of small peptides in addition to regular structures. Thus, the methods uses both the regular secondary structure information predicted from PSIPRED and β-turns information predicted from BetaTurns. The side-chain abgles are placed using standard backbone-dependent rotamer library. The structure is further refined with energy minimization and molecular dynamic simulations using Amber version6.