title: 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.
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.
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: Joseph Dale
authors.initials: JD
authors.lastname: Combs
authors.forename: Olaa Eid
authors.initials: OE
authors.lastname: Alharbi
authors.forename: Jing
authors.initials: J
authors.lastname: Kong
authors.forename: Chengshan
authors.initials: C
authors.lastname: Wang
authors.forename: Roger M
authors.initials: RM
authors.lastname: Leblanc
mesh_terms: D000577:Amides / Q000737:chemistry*; D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D002942:Circular Dichroism; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared; D014867:Water / Q000737:chemistry*
chemical_list: D000577:Amides; D002247:Carbon Isotopes; D010455:Peptides; D014867:Water