Hydrogen Bonding in Proteins and Water Studied by Far‐IR and Low‐Wavenumber Raman Spectroscopy
- Conference date: 24–28 February 2008
- Location: Thiruvananthapuram, Kerala (India)
Far‐IR spectra with a synchrotron radiation source were for the first time recorded through a microscope coupled to an FTIR‐spectrometer. A comparison with spectra recorded with an ordinary globar source revealed that no artifacts occurred with synchrotron radiation. A comparison of ATR (Si‐prism) and transmission spectra of a tetrapeptide showed that the ATR‐microscope technique could be applied. ATR‐ and transmission spectra were recorded of polyglycine and compared to the low wavenumber Raman spectrum in the ‐representation. A protein band at was assigned to hydrogen bond modes. Collectively these modes might drive conformational changes in proteins. Based mainly on previously published results the determination of water with a structure like that in bulk liquid water was performed for human and animal skin samples. Changes in water content were reported for freezing and thawing of human skin biopsies and for human skin with benign or malignant skin diseases.
- Raman spectra
- Hydrogen bonding
- Synchrotron radiation
- Attenuated total reflection
- Radioactive sources
- Raman spectroscopy
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