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Calculated Raman Optical Activity Signatures of Tryptophan Side Chains
Author(s) -
Jacob Christoph R.,
Luber Sandra,
Reiher Markus
Publication year - 2008
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.200800448
Subject(s) - raman optical activity , tryptophan , side chain , raman spectroscopy , chemistry , chirality (physics) , pendant group , aromatic amino acids , stereochemistry , amino acid , crystallography , chiral symmetry , optics , organic chemistry , physics , polymer , biochemistry , quantum mechanics , nambu–jona lasinio model , quark
Raman optical activity: The different local chirality of an adjacent group can cause a different sign of the ROA intensity of an amino‐acid side chain (here tryptophan, see picture centre), even though the normal mode is unchanged. Calculated spectra clearly confirm that ROA spectroscopy can be utilized to determine the absolute conformation of tryptophan side chains in proteins (see figure, left and right).