Abstract
We show that perdeuterated side chain of leucine amino acid and related compounds can serve as a useful structural reporter, suitable for studying proteins using two-dimensional infrared (2DIR) spectroscopy. Strong direct-coupling C-D/C=O and C-D/Am-II cross-peaks were measured by dual-frequency 2DIR in these compounds. The direct-coupling cross peaks were further enhanced up to 5 fold using the relaxation-assisted 2DIR method. The energy transport times (arrival times) and amplification factors were measured and used to assign the C-D absorption peaks and these assignments were compared with the results of anharmonic DFT calculations.KeywordsArrival TimeCross PeakEster HydrochlorideLinear SpectrumLeucine Amino AcidThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
Published Version
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