中国物理B ›› 2005, Vol. 14 ›› Issue (11): 2365-2369.doi: 10.1088/1009-1963/14/11/038
盛乐标1, 李菁1, 马保亮1, 王炜2
Sheng Yue-Biao (盛乐标)a, Li Jing (李菁)a, Ma Bao-Liang (马保亮)a, Wang Wei (王炜)ab
摘要: The folding dynamics and structural characteristics of peptides RTKAWNRQLYPEW (P1) and RTKQLYPEW (P2) are investigated by using all-atomic simulation procedure CHARMM in this work. The results show that P1, a segment of an antigen, has a folding motif of α-helix, whereas P2, which is derived by deleting four residues AWNR from peptide P1, prevents the formation of helix and presents a β-strand. And peptide P1 experiences a more rugged energy landscape than peptide P2. From our results, it is inferred that the antibody CD8 cytolytic T lymphocyte prefers an antigen with a β-folding structure to that with an α-helical one.
中图分类号: (Structure of biomolecules)