Isotope-edited FTIR in H2O: Determination of the conformation of specific residues in a model α-helix peptide by 13C labeled carbonyls

Shanghao Li, Sneha Potana, Donnan J. Keith, Chengshan Wang, Roger Leblanc

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Isotope-edited FTIR spectroscopy has been shown to be able to determine peptide's structure in the residue level in D2O, which is not a physiological solvent. Here, attenuated total reflection technique was utilized to successfully apply isotope-edited FTIR spectroscopy in H2O to determine the conformation of specific residues in a model peptide.

Original languageEnglish
Pages (from-to)3931-3933
Number of pages3
JournalChemical Communications
Volume50
Issue number30
DOIs
StatePublished - Apr 18 2014

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Isotopes
Peptides
Conformations
Spectroscopy

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Ceramics and Composites
  • Electronic, Optical and Magnetic Materials
  • Surfaces, Coatings and Films
  • Materials Chemistry
  • Metals and Alloys

Cite this

Isotope-edited FTIR in H2O : Determination of the conformation of specific residues in a model α-helix peptide by 13C labeled carbonyls. / Li, Shanghao; Potana, Sneha; Keith, Donnan J.; Wang, Chengshan; Leblanc, Roger.

In: Chemical Communications, Vol. 50, No. 30, 18.04.2014, p. 3931-3933.

Research output: Contribution to journalArticle

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