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 M Leblanc

doi:10.1039/c4cc00991f

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

Chem Commun (Camb). 2014 Apr 18;50(30):3931-3. doi: 10.1039/c4cc00991f. Epub 2014 Mar 5.

Authors

Shanghao Li¹, Sneha Potana, Donnan J Keith, Chengshan Wang, Roger M Leblanc

Affiliation

¹ Department of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, Fl 33146, USA. [email protected].

PMID: 24595891
DOI: 10.1039/c4cc00991f

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.

Publication types

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

MeSH terms

Carbon Isotopes
Peptides / chemistry*
Protein Conformation
Spectroscopy, Fourier Transform Infrared
Water / chemistry*

Substances

Carbon Isotopes
Peptides
Water