期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 133, 期 19, 页码 7300-7303出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja201349g
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资金
- Czech Science Foundation [203/08/0114]
- Ministry of Education [LC 512]
- Academy of Sciences (Praemium Academie)
The effects of chloride and sulfate salts of tetrapropylammonium (TPA(+)) and guanidinium (Gdm(+)) on the conformational stabilities of tryptophan zipper (trpzip) and alpha-helical (alahel) peptides were measured by circular dichroism spectroscopy. Like Gdm(+), TPA(+) interacts with the planar tryptophan indole group, perturbing the conformational stability of trpzip peptides. TPA(+) effects are largely unaffected by sulfate, indicating an absence of the heteroion pairing that is observed in concentrated Gdm(2)SO(4) solutions. TPA(+) stabilizes helical conformations in alahel peptides, indicating exclusion from the peptide bond. The observations are broadly consistent with predictions of molecular dynamics simulations [Mason, P. E.; et al. J. Phys. Chem. B 2009, 113, 3227-3234], indicating that the effects of complex ions on proteins are increasingly predictable in terms of ion hydration, complementary interactions with specific protein groups, and ion-pairing contributions.
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