Two-dimensional infrared spectroscopy displays signatures of structural ordering in peptide aggregates.

@article{Londergan2006TwodimensionalIS,
  title={Two-dimensional infrared spectroscopy displays signatures of structural ordering in peptide aggregates.},
  author={Casey H Londergan and Jianping Wang and Paul H. Axelsen and Robin M. Hochstrasser},
  journal={Biophysical journal},
  year={2006},
  volume={90 12},
  pages={4672-85}
}
In the presence of lipid bilayers, the hexapeptide AcWL(5) forms membrane-bound aggregates dominated by beta-secondary structure and is thus a useful model for the onset of peptide aggregation in membrane environments. Two-dimensional infrared (2D IR) spectra in the amide I region for aggregates of AcWL(5) peptides with single isotopic labels provide new insight into the residue-level structural ordering of the aggregated peptides. Separation of spectral information along two axes provides… CONTINUE READING

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\ Two - dimensional infrared spectroscopy displays signatures of stuctural ordering in peptide aggregates

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