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Variation in proton affinity of the guanidino group between free and blocked arginine

机译:游离和封闭精氨酸之间胍基的质子亲和力变化

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In this paper,the analog of arginine residues in peptides was synthesized and characterized by ESI-MS/MS(electrospray ionization with tandem mass spectrometry),~(31)P NMR,~1H NMR,IR and high-resolution mass spectrometry.When the Todd reaction activity of the guanidino group in free arginine and the arginine peptide analog were compared,it was found that the proton affinity of the guanidino group was decreased when both the N-and the C-terminal were blocked.As a result,the guanidino group of arginine residues in peptides could be phosphorylated under the Todd reaction condition,but not the free arginine.This result was further proved by the theoretical calculation of their proton affinity.
机译:本文通过ESI-MS / MS(串联质谱电喷雾电离),〜(31)P NMR,〜1H NMR,IR和高分辨质谱对肽中精氨酸残基的类似物进行了合成和表征。比较了游离精氨酸和精氨酸肽类似物中胍基的托德反应活性,发现当N-和C-末端均被封闭时,胍基的质子亲和力降低。肽中的精氨酸残基的胍基在托德反应条件下可以被磷酸化,而游离精氨酸则不能被磷酸化。这一结果通过其质子亲和力的理论计算得到了进一步证明。

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