ArticleJournal of Raman spectroscopy : JRS2012
UV resonance Raman study of TrpZip2 and related peptides: π-π interactions of tryptophan.
Article in Journal of Raman spectroscopy : JRS, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 8 citations in OpenAlex.
- Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy.Biochemistry · 2015Article
- Correct folding of an α-helix and a β-hairpin using a polarized 2D torsional potential.Scientific reports · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Aromatic interactions are important stabilizing forces in proteins but are difficult to detect in the absence of high-resolution structures. Ultraviolet resonance Raman spectroscopy is used to probe the vibrational signatures of aromatic interactions in TrpZip2, a synthetic β-hairpin peptide that is stabilized by edge-to-face and face-to-face tryptophan π-π interactions. The vibrational markers of isolated edge-to-face π-π interactions are investigated in the related β-hairpin peptide W2W11. The bands that comprise the Fermi doublet exhibit systematic shifts in position and intensity for TrpZip2 and W2W11 relative to the model peptide, W2W9, which does not form aromatic interactions. Additionally, hypochromism of the B
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