Based on MD simulations, we calculated the conformational entropies of a designed 10-residue peptide, or the mini-protein Chignolinpsilas eight residues (2-9) at four different temperature. Our results show that five conformational entropies of Chignolinpsilas eight residues have different jump. At 260 K, the conformational entropy of Gly(7) generates three orders jump, which are being founded and that of Thr(8) generates one order jump; at 300 K, the conformational entropies of Asp(3), Pro(4), and Thr(8) generates two orders jump; at 400 K, the conformational entropies of Asp(3), Pro(4), Thr(6) and Thr(8) generates one order jump. The curves of conformational entropies are coincident with RMSD, however the convergence of the conformational entropies by comparing the former with the latter and this shows conformational entropies can illustrate the changes of conformations very well. The main factors influence on the residue conformational entropies are also discussed in this paper.