英语翻译The three-dimensional structures in dodecylphosphocholine (DPC) micelles and in trifluoroethanol (TFE) of the pediocin-like antimicrobial peptide sakacin P and an engineered variant of sakacinP (termed sakP[N24C+44C]) have been determined

英语翻译The three-dimensional structures in dodecylphosphocholine (DPC) micelles and in trifluoroethanol (TFE) of the pediocin-like antimicrobial peptide sakacin P and an engineered variant of sakacinP (termed sakP[N24C+44C]) have been determined
英语翻译
The three-dimensional structures in dodecylphosphocholine (DPC) micelles and in trifluoroethanol (TFE) of the pediocin-like antimicrobial peptide sakacin P and an engineered variant of sakacinP (termed sakP[N24C+44C]) have been determined by use of nuclear magnetic resonance spectroscopy.SakP[N24C+44C] has an inserted non-native activity- and structure-stabilizing C-terminal disulfide bridge that ties the C-terminus to the middle part of the peptide.In the presence of DPC,the cationic N-terminal region (residues 1-17) of both peptides has an S-shaped conformation that is reminiscent of a three stranded antiparallel â-sheet and that is more pronounced when the peptide was dissolved in TFE instead of DPC.The four positively charged residues located in the N-terminal part are found pointing to the same direction.For both peptides,the N-terminal region is followed by a well-defined central amphiphilic R-helix (residues 18-33),and this in turn is followed by the C-terminal tail (residues 34-43 for sakacinP and 34-44 for sakP[N24C+44C]) that lacks any apparent common secondary structural motif.In the presence of DPC,the C-terminal tails in both peptides fold back onto the central R-helix,thereby creating a hairpin-like structure in the C-terminal halves.The lack of long-range NOEs between the â-sheet Á-terminal region and the hairpin-like C-terminal half indicates that there is a flexible hinge between these regions.We discuss which implications such a structural arrangement has on the interaction with the target cell membrane.

英语翻译The three-dimensional structures in dodecylphosphocholine (DPC) micelles and in trifluoroethanol (TFE) of the pediocin-like antimicrobial peptide sakacin P and an engineered variant of sakacinP (termed sakP[N24C+44C]) have been determined
在dodecylphosphocholine的三维结构（缩节胺）胶束和三氟乙醇的pediocin样抗菌肽sakacin P和一个sakacinP工程变种（称为sakP [N24C 44 ç]）（四氟乙烯）已经通过使用核磁共振确定光谱.SakP [N24C 44 ç]有一个插入非本地活动和结构,稳定的C -末端二硫桥关系的C -末端的肽的中间部分.在DPC的存在,阳离子的N -末端区（1-17残留两个肽）有一个S形构象,它是一个三股反平行â页回忆,这是更加明显,当肽在TFE解散而缩节胺.在这四个正电荷的N -末端残基,位于被发现指向同一方向.对于这两种肽的N -末端区之后是一个明确的中央双亲的R -螺旋（残基18-33）,这又是由C端尾巴（残基34-43遵循sakacinP和34 - 44 sakP [N24C 44 ç]）表示,没有任何明显的二级结构的共同主题.在DPC的存在,在这两个多肽的C端尾巴折返回到中央的R -螺旋,从而创造一个在C端半发夹样结构.长程等NOE之间的A片给终端区和发夹状结构的C -端半缺乏表明,两者之间是有这些地区灵活的铰链.我们将讨论哪些问题上这样的结构安排与目标细胞的细胞膜相互作用.（机器翻译）

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