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Kinetics, Spectroscopy
Utilizing Lifetimes to Suppress Random Coil Features in 2D IR Spectra of Peptides
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Section:Abstract
We report that the waiting time delay in 2D IR pulse sequences can be used to suppress signals from structurally disordered regions of amyloid fibrils. At a waiting time delay of 1.0 ps, the random coil vibrational modes of amylin fibrils are no longer detectable, leaving only the sharp excitonic vibrational features of the fibril β-sheets. Isotope labeling with 13C18O reveals that structurally disordered residues decay faster than residues protected from solvent. Because structural disorder is usually accompanied by hydration, we conclude that the shorter lifetimes of random-coil residues are due to solvent exposure. These results indicate that 2D IR pulse sequences can utilize the waiting time to better resolve solvent-protected regions of peptides and that local mode lifetimes should be included in simulations of 2D IR spectra.
Keywords:
protein and peptide structure; 2D IR spectroscopy; secondary structure; vibrational lifetimes; amide-I vibration; isotope labeling; amyloid fibrils; amylinTools
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History
- Published In Issue September 15, 2011
- Article ASAPAugust 31, 2011
- Just Accepted ManuscriptAugust 25, 2011
- Received: July 28, 2011
Accepted: August 25, 2011
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