B. Liedberg, C. Tornkvist, I. Lundstrom
Dec 1, 1989
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Abstract
Infrared reflection-absorption spectroscopy (IRAS) and attenuated total reflection (ATR) spectroscopy have been used to investigate the bonding characteristics of N-methylacetamide (NMAA) on solid surfaces with different surface energies. Infrared spectra of monomolecular layers on hydrophilic (clean) surfaces suggest that the -C=N- nature or dipolar form of the peptide bond partly remains on the surface because of hydrogen-bond interaction with surfaces hydroxyls or adsorbed water molecules, whereas no such interaction occurs on hydrophobic (alkyl-modified) surfaces. The results obtained for the hydrophobic surfaces indicate that the -C=N- axis of the peptide bond becomes more notable, a phenomenon which for protein molecules may lead to a loosening of the backbone structure and a more unstable conformation.