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your2007至尊木虫 (著名写手)
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Interactions of casein signal peptides (CSP) and derivatives were detected with dimyristoylphosphatidyl-glycerol and -choline liposomes. Fluorescence anisotropy indicated that the peptides interact better with DMPG than DMPC, inserting at a limited depth in the bilayer. Stronger interaction was detected for derivatives of b-CSP than of as2-CSP. Tryptophan fluorescence ( intrinsic, energy transfer, quenching) showed that the central hydrophobic core of CSP was buried in the bilayer whereas both ends remained outside, adopting a hairpin-like conformation. The secondary structure of the CSP was not affected by their interactions with phospholipids. b-CSP derivatives show both lytic and fusogenic activities. |
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xiangyi007
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爱与雨下: 金币+1 2012-12-24 21:55:29
your2007: 金币+15, 翻译EPI+1, ★★★★★最佳答案, 谢谢 2012-12-25 08:13:02
爱与雨下: 金币+1 2012-12-24 21:55:29
your2007: 金币+15, 翻译EPI+1, ★★★★★最佳答案, 谢谢 2012-12-25 08:13:02
| 酪蛋白信号肽（CSP）和派生物之间的相互作用利用二肉豆蔻酰磷脂酰和胆碱脂质体检测到。荧光各向异性表明嵌入双分子层一定深度的多肽和二肉豆蔻酰磷脂酰甘油之间反应比和二肉豆蔻酰磷脂酰胆碱的好。b-CSP派生物比2-CSP派生物有更强的反应。色氨酸荧光（内部的、能量传递、淬火）显示CSP的中心疏水内芯为双分子层包裹，两端都露出，采取发夹式构造。CSP的二级结构不受和磷脂质相互作用的影响。b-CSP派生物表明裂解和膜融合。 |
2楼2012-12-24 14:54:42