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Proline-glutamate chimera's side chain conformation directs the type of P-hairpin structure

机译:脯氨酸-谷氨酸嵌合体的侧链构象指导P-发夹结构的类型

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Our aim was to study the impact of two proline chimeras, containing a glutamic acid side chain in cis-or trans-configuration, on secondary structure formation. We further investigated to what extent the configuration of the side chain contributes to the overall peptide conformation. We used a 10 residue peptide (IYSNPDGTWT) that forms a P-hairpin in water. The turn-forming proline was substituted with either a cis-or rrans-proline-glutamic acid chimera, resulting in the peptides IYSNP~(cis-E)DGTWT (Pl_P~(cis-E)) and IYSNP~(trans-E)DGTWT (P1_P~(trans-E)). We studied the conformation of the modified peptides by circular dichroism (CD) and NMR-spectroscopy, and SEC/ static light scattering (SLS) analysis. NMR analysis reveals that the modified peptides maintain the P-hairpin conformation in aqueous solution. At 5 °C and pH 4.3, the peptide (Pl_P~(cis-E) was found to adopt two coexisting P-hairpin conformations (2:2 p-hairpin, and 3:5 P-hairpin). In contrast to that, the peptide (p1_p~(trans-E)) adopts a 2:2 P-hairpin that exists in equilibrium with a 4:4 P-hairpin conformation. The adoption of ordered p-hairpin structures for both modified peptides could be confirmed by CD spectroscopy, while SEC/SLS analysis showed a mono-meric oligomerization state for all three investigated peptides. With the combination of several NMR methods, we were able to elucidate that even small alterations in the side chain conformation of the proline-glutamate chimera (cis or trans) can significantly influence the conformation of the adopted P-hairpin.
机译:我们的目的是研究两个脯氨酸嵌合体,其中谷氨酸侧链为顺式或反式构型,对二级结构形成的影响。我们进一步研究了侧链的构型在多大程度上有助于整体肽构象。我们使用了10个残基的肽(IYSNPDGTWT),它在水中形成P型发夹。用顺-或兰-脯氨酸-谷氨酸嵌合体取代形成轮状的脯氨酸,得到肽IYSNP-(顺式-E)DGTWT(P1-P-(顺式-E))和IYSNP-(反式-E) DGTWT(P1_P〜(trans-E))。我们通过圆二色性(CD)和NMR光谱以及SEC /静态光散射(SLS)分析研究了修饰肽的构象。 NMR分析表明,修饰的肽在水溶液中保持P-发夹构象。在5°C和pH 4.3下,发现该肽(Pl_P〜(cis-E)具有两个并存的P-发夹构象(2:2 p-发夹和3:5 P-发夹)。肽(p1_p〜(trans-E))采用2:2 P-发夹,并以4:4 P-发夹构象平衡存在,两种修饰肽的有序p-发夹结构均可通过CD确认。光谱,而SEC / SLS分析显示了所有三种研究肽段的单体低聚状态。结合几种NMR方法,我们可以阐明脯氨酸-谷氨酸嵌合体的侧链构象即使很小的变化(顺式或反式)可以显着影响所采用的P型发夹结构。

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