Structure of protonated tryptophan dimer in the gas phase investigated by IRPD spectroscopy and theoretical calculations.

Abstract

In addition to proton affinity (PA), side chains may also have an effect on the structures of amino acid complex ions in the gas phase. A previous study showed that the most stable isomer of Pro2 H(+) favored a salt-bridged structure. Tryptophan has a PA close to that of proline, but a quite different side chain. Thus, it will be interesting to discover whether the salt-bridged or charge-solvated conformation is energetically more favorable for Trp2 H(+) in the gas phase. The infrared photodissociation (IRPD) spectrum of Trp2 H(+) was obtained using a Fourier transform ion cyclotron resonance mass spectrometer equipped with a tunable OPO laser. The non-covalent cluster ions were generated by electrospray ionization. Structural optimization and frequency calculation of the selected isomers were performed at the M062X/6-311++G(d,p) level. The experimental IRPD spectrum of Trp2 H(+) was reported in the region of 2700-3750cm(-1) . Theoretical calculations show that the most stable isomer has a charge-solvated structure. Its energy was found to be 9kcal/mol lower than that of the most stable salt-bridged isomer. The experimental spectrum is consistent with the predicted spectra of the most stable charge-solvated structures. Temperature effect on the stability of isomers was also evaluated and it was revealed that the contribution from salt-bridged isomers can be neglected at a temperature of 300K. Combining the method of IRPD spectroscopy with theoretical calculations, the structures of Trp2 H(+) were investigated. It is shown that the structures of Trp2 H(+) are dominated by charge-solvated forms. The results also indicate that the side chain may considerably affect the stability of the zwitterionic forms. Copyright © 2016 John Wiley & Sons, Ltd.