1 December 1989 An Infrared Study Of N-Methylacetamide On Solid Surfaces: A Model Molecule For The Peptide Group In Proteins
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Proceedings Volume 1145, 7th Intl Conf on Fourier Transform Spectroscopy; (1989) https://doi.org/10.1117/12.969395
Event: Seventh International Conference on Fourier and Computerized Infrared Spectroscopy, 1989, Fairfax, VA, United States
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.
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Bo Liedberg, Christer Tornkvist, Ingemar Lundstrom, "An Infrared Study Of N-Methylacetamide On Solid Surfaces: A Model Molecule For The Peptide Group In Proteins", Proc. SPIE 1145, 7th Intl Conf on Fourier Transform Spectroscopy, (1 December 1989); doi: 10.1117/12.969395; https://doi.org/10.1117/12.969395
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