Raman signature of the non-hydrogen-bonded tryptophan side chain in proteins: experimental and ab initio spectra of 3-methylindole in the gas phase

3-Methylindole (3MI), which serves as a structural model for the tryptophan side chain in proteins. has been investigated using vapor phase Raman spectroscopy. The vapor phase spectrum of 3MI identifies the Raman signature of the indolyl moiety firee of intermolecular interaction and extends previously reported solution Raman studies of 3MI and related tryptophan derivatives. The Raman spectrum of 3MI vapor is also complemented here with newly obtained vapor phase infrared data and ab initio calculations to refine and extend previous vibrational assignments. The present results provide an improved basis for assessing the dependence of the indolyl Raman signature on the local environment of the tryptophan side chain of proteins. The principal conclusions of this work are the following. W The vapor phase 3MI molecule exhibits Raman bands at 3506, 1585, 1409, 1349/1341 (Fermi doublet) and 881 cm(-1). which differ greatly from their counterparts in the Raman spectrum of 3MI liquid and thus serve as spectral markers of the indolyl ring environment. (ii) The Fermi doublet relative intensity ratio (I1II2, where I-1 and I-2 are, respectively, the Raman intensifies of the higher and lower wavenumber components of the doublet)) is highly sensitive to the state of 3MI condensation, consistent with the previously reported sensitivity of I1II2 to solvent polarity. The maximum value of the intensity ratio (I1II2 = 3.0) is observed for 3MI vapor, while the minimum value (I1II2 = 3.0) is observed for 3MI in CHCl3 solution. Implications of the present results for Raman analysis of hydrogen bonding states. hydrophilic interactions and hydrophobic interactions of tryptophan residues in proteins are considered. (C) 2004 Elsevier B.V. All rights reserved.