title: Isotope-edited FTIR in H2O: determination of the conformation of specific residues in a model α-helix peptide by 13C labeled carbonyls.
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.
authors.affiliation: Department of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, Fl 33146, USA. rml@miami.edu.
authors.forename: Shanghao
authors.initials: S
authors.lastname: Li
authors.forename: Sneha
authors.initials: S
authors.lastname: Potana
authors.forename: Donnan J
authors.initials: DJ
authors.lastname: Keith
authors.forename: Chengshan
authors.initials: C
authors.lastname: Wang
authors.forename: Roger M
authors.initials: RM
authors.lastname: Leblanc
mesh_terms: D002247:Carbon Isotopes; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017550:Spectroscopy, Fourier Transform Infrared; D014867:Water / Q000737:chemistry*
chemical_list: D002247:Carbon Isotopes; D010455:Peptides; D014867:Water