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

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

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 conformati...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2015-08, Vol.51 (63), p.12537-12539
Hauptverfasser: Li, Shanghao, Combs, Joseph Dale, Alharbi, Olaa Eid, Kong, Jing, Wang, Chengshan, Leblanc, Roger M
Format: Artikel
Sprache:eng
Schlagworte:
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
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Zusammenfassung: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.
ISSN:1364-548X
DOI:10.1039/c5cc02263k