The (13)C amide I band is still sensitive to conformation change when the regular amide I band cannot be distinguished at the typical position in H2O

Chem Commun (Camb). 2015 Aug 14;51(63):12537-9. doi: 10.1039/c5cc02263k.

Abstract

The attenuated total reflection technique was utilized to obtain FTIR spectra of (13)C-labeled peptides with a sequence of (AAAAK)4AAAAY in H2O. The regular amide I band was not at the typical position as reported in globular proteins, whereas the (13)C amide I band was still sensitive to conformation change.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amides / chemistry*
  • Amino Acid Sequence
  • Carbon Isotopes / chemistry
  • Circular Dichroism
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Peptides / metabolism
  • Protein Structure, Secondary
  • Spectroscopy, Fourier Transform Infrared
  • Water / chemistry*

Substances

  • Amides
  • Carbon Isotopes
  • Peptides
  • Water