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首页> 外文期刊>The journal of physical chemistry, A. Molecules, spectroscopy, kinetics, environment, & general theory >Photodissociation and spectroscopic study of cold protonated dipeptides
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Photodissociation and spectroscopic study of cold protonated dipeptides

机译：冷质子化二肽的光解离和光谱研究

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A photodissociation spectrometer, containing a spray ionization source and a temperature-variable multipole ion trap, has been constructed to examine the structure and reactivity of gas phase biological molecular ions at various temperatures. Ultraviolet (UV) and infrared (IR) photodissociation spectra of protonated alanyltryptophan (Ala-TrpH(+)) and tryptophanylglycine (Trp-GlyH(+)) have been measured. In UV spectra, the S-1-S-0 band origin of Ala-TrpH(+) exhibits a significant red shift with respect to those of protonated tryptophan (TrpH(+)) and Trp-GlyH(+). This red shift is ascribed to the stabilization of the excited state due to the strong interaction between the NH3+ group and indole ring. We also discuss the temperature effect on the structure and reactivity for these peptides. In addition to the UV photodissociation spectra of the dipeptides, IR spectra of the complex of Ala-TrpH(+) with methanol are measured. IR photodissociation spectra of solvated ions show that Ala-TrpH(+)-methanol has the closed structure, which is consistent with the large spectral shift in UV spectrum of bare dipeptide.
机译：已经构造了包含喷雾电离源和温度可变的多极离子阱的光解离光谱仪，以检查在各种温度下气相生物分子离子的结构和反应性。已测量了质子化的丙氨酰色氨酸（Ala-TrpH（+））和色氨酸甘氨酸（Trp-GlyH（+））的紫外（UV）和红外（IR）光解离光谱。在紫外光谱中，相对于质子化色氨酸（TrpH（+））和Trp-GlyH（+）而言，Ala-TrpH（+）的S-1-S-0谱带起源表现出显着的红移。这种红移归因于由于NH3 +基团与吲哚环之间的强相互作用而激发态的稳定。我们还讨论了温度对这些肽的结构和反应性的影响。除了二肽的紫外光解离光谱外，还测量了Ala-TrpH（+）与甲醇的配合物的IR光谱。溶剂化离子的红外光解离光谱表明，Ala-TrpH（+）-甲醇具有封闭的结构，这与裸露的二肽的UV光谱中的大光谱位移一致。

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