STUDYING THE ENERGY LANDSCAPE OF AN ALPHA HELIX USING 2D IR SPECTROSCOPY

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Two-dimensional infrared spectroscopy (2D IR) is capable of measuring the vibrational coupling between amide groups, analogous to 2D NMR measuring nuclear spin coupling. Because the coupling is sensitive to the peptide's 3D structure, the cross peaks observed in 2D IR should tell us about the peptide's secondary and tertiary structure. In this way, we should be able to monitor the motions of localized pieces of the alpha-helix, and relate these motions to changes in structure. In conjunction with simulations, this technique will reveal a much more detailed insight into the intra-peptide vibrational coupling and its structural significance. We propose to insert isotopically labels (13C=16O and 13C=18O) into alpha-helix model peptides to study experimentally (using 2D-IR techniques) the impact of structural motives on vibrational coupling.