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Additional resources for Principles of mass spectrometry applied to biomolecules
In the case of Ac–Phe–OMe only an inner-bound b-sheet arrangement can be formed and has been experimentally determined (Gerhards and Unterberg 2002; Gerhards et al. 2002). It is significant that more than one inner- or outer-bound dimer can be formed; three possible orientations of the sidechain (gþ, gÀ, a) for each monomer yield nine possible inner- or outer-bound dimer structures. 11. 10: (a) for the dimer of Ac–Phe–OMe an inner-bound arrangement has been observed (Gerhards et al. 2002; Gerhards and Unterberg 2002); (b) in the case of Ac–Phe–NHMe both inner- and outer-bound structures are possible but only the outer-bound arrangement has been observed experimentally (Gerhards et al.
IR/R2PI spectra of three isomers of Trp in the fingerprint and amide II region from 330 to 1500 cmÀ1 (Bakker et al. 2003). The experimental spectra (upper traces) are compared to the calculated spectra (lower trace) obtained at DFT [B3LYP/6-31 þ G(d)] level. These spectra are given both as stick spectrum and as convolution with the spectral profile of the free-electron laser (Oepts et al. 1994). The corresponding structures of isomers A, D, and E are given at the bottom (for further details, see text).
2005), who recorded the rotationally resolved laser-induced fluorescence spectrum of six monomer conformers and the monohydrated cluster of tryptamine and observed, in combination with ab initio calculations, an additionally stabilizing interaction of water with one of the aromatic CÀ ÀH bonds. This leads to a situation where the energy difference to all other possible clusters of tryptamine with water is much higher than between the different monomers. The very similar melantonin (N-acetyl-5-methoxytryptamine) and its cluster with water has also been investigated via IR/UV spectroscopy (Florio et al.