Coherent control of bond breaking in amino acid complexes with tailored femtosecond pulses
Coherent control of bond breaking in amino acid complexes with tailored femtosecond pulses
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DOI：
10.1063/1.2806029
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发表时间：
2007-11-28
影响因子：
4.4
通讯作者：
Hertel, I. V.
中科院分区：
文献类型：
--
作者：
Laarmann, T.;Shchatsinin, I.;Hertel, I. V.
强烈的飞秒激光脉冲，明智地定制在一个自适应的，最佳的控制反馈回路被用来优先打破酰基-N（“肽”）键的Ac-Phe-NHMe，可以被视为一个二肽模型。我们表明，相干激发的复杂波包在强场制度允许裂解强骨干键的分子系统优先，同时保持其他更不稳定的债券完整。这些结果表明，除了众所周知的质谱和化学分析之外，脉冲整形作为大型生物聚合物蛋白质测序的强大补充分析工具的潜力。(c)2007年，美国物理学会。
Intense femtosecond laser pulses, judiciously tailored in an adaptive, optimal control feedback loop were used to break preferentially the acyl-N ("peptide") bond of Ac-Phe-NHMe that may be regarded as a dipeptide model. We show that coherent excitation of complex wave packets in the strong-field regime allows to cleave strong backbone bonds in the molecular system preferentially, while keeping other more labile bonds intact. These results show the potential of pulse shaping as a powerful complementary analytical tool for protein sequencing of large biopolymers in addition to the well-known mass spectrometry and chemical analysis. (c) 2007 American Institute of Physics.