The dynamics character of H1 peptide in aqueous solution at different temperatures has been investigated through temperature replica exchange molecular dynamics (T-REMD) simulations with GROMOS 43A1 force field. The two independent T-REMD simulations were completed from initial conformations α-helix and β-sheet structures, respectively. Each replica was run for 300 ns. 36 replicas have been simulated and the total MD simulation time of all replicas was 21.6 ?滋s, the convergence of conformation sampling was verified by simulations starting from β-sheet structure. The structural character of H1 peptide at each temperature (300K, 330K, 350K and 370K) was assessed from the parameters such as the distributions of backbone dihedral angles, the number of native hydrogen bond, formation of β-turn and the favorite conformation at different temperatures. The simulations sampled conformation cluster close to β-sheet structure as demonstrate by the 0.05 nm Cα RMSD, and this cluster contains 39%, 23%, 13% and 11% conformations in total at 300K, 330K, 350K and 370K respectively. The results indicate that: GROMOS 43A1 force field has precision of the description of the conformational equilibriums, however, efforts have been made to refine the treatments of hydrogen bond, and the comparative study of H1 peptide at different temperatures can afford information for refine molecular force field.