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Singly Protonated Tryptic Peptides with Penultimate Proline: Isomerization is the Gateway to Fragmentation

机译:单位质子化的胰蛋白胨含有倒数二脯氨酸:异构化是碎片的门户

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We investigate singly protonated glycylprolylarginine, [GPR+H]~+, a simple model system for the fragmentation behavior of tryptic peptides and the proline effect. H~+ mobilization in arginine-containing, [M+H]~+, systems is complex: Mobilization from either the guanidino side-chain of arginine or the C-terminal acid (salt-bridge). Isomerization to anhydride structures. Proline also exhibits residue-specific chemistry. Preferential fragmentaion at the prolyl N-terminus => y_m ions. Trans to cis isomerization of the amide bond is facilitated by proline. Here we investigate the competition between these chemistries.
机译:我们研究了单独质子糖基脯氨酸,[GPR + H]〜+,一种简单的模型系统,用于胰蛋白酶肽的碎片行为和脯氨酸作用。 H〜+在含精氨酸的[M + H]〜+中的动员,系统复杂:从精氨酸或C-末端酸(盐桥)的胍酰胺侧链的动员。对酸酐结构的异构化。脯氨酸还表现出残留物特异性化学。在N-Terminus => Y_m离子的优选碎片化。通过脯氨酸促进酰胺键的反式酰胺键。在这里,我们调查这些化学物质之间的竞争。

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