期刊
BIOCHEMISTRY
卷 39, 期 45, 页码 13737-13747出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi001126b
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资金
- NIGMS NIH HHS [R29-GM52431] Funding Source: Medline
Molecular dynamics simulations were carried out for three 13-residue peptides of the form AcNH-A-A-E-X-A-E-A-H-A-A-E-K-A-CONH2 with X = A, F, and W. All three peptides exhibited unexpected dynamical behavior, undergoing a transition from an alpha -helical to a pi -helical structure in the course of 5-ns trajectories in aqueous solution. Analysis of peptide length, accessible surface, interaction energies, hydrogen bonding, and dihedral angles was consistent with alpha --> pi transitions at 2800, 500, and 800 ps for X = A, F and W, respectively. The transitions occurred sequentially and cooperatively, propagating from the C- to the N-terminus for X = A and W and from the center toward both termini for X = F. The time scale of the overall transition ranged from 300 to 500 ps. For all three peptides the backbone structural transition was accompanied by a concerted rearrangement of the charged side chains, including a 3 Angstrom increase in the distance between carboxylate groups of Glu-3 and Glu-6. During the transition the peptide backbone hydrogen-bonding patterns were disrupted at the interface between the alpha -helical and nascent pi -helical regions, with peptide groups forming water-bridged hydrogen bonds. The peptide structures exhibited significant fluidity, with individual residues sampling alpha-, pi-, and 3(10)-helical conformations, as well as a coil state, without any intramolecular hydrogen bonds. The studied peptides have been designed to form alpha -helices when incorporated in novel hemoprotein model compounds, peptide-sandwiched mesohemes, which consist of two identical peptides covalently attached to an Fe(III) mesoporphyrin [Liu, D., Williamson, D. A., Kennedy, M. L., Williams, T. D., Morton, M. M., and Benson, D. R. (1999) J. Am. Chern. Sec. 121, 11798-11812]. The possibility of adopting pi -helical structures by the constituent peptides may influence the properties of the hemoprotein models.
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