Coherent control of bond breaking in amino acid complexes with tailored femtosecond pulses.

Autor: Laarmann, T., Shchatsinin, I., Singh, P., Zhavoronkov, N., Gerhards, M., Schulz, C. P., Hertel, I. V.
Předmět:
Zdroj: Journal of Chemical Physics; 11/28/2007, Vol. 127 Issue 20, p201101, 4p, 2 Diagrams, 2 Graphs
Abstrakt: 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. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index