2001
DOI: 10.1016/s0167-4838(01)00201-1
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Calorimetric and Fourier transform infrared spectroscopic study of solid proteins immersed in low water organic solvents

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Cited by 72 publications
(38 citation statements)
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“…Among these amide bands amide I and amide II are more important. Amide I band originates between 1600 and 1700 cm −1 and is due to the C O stretching while amide II band appears in between 1500 and 1600 cm −1 owing to the C N stretching coupled with N H bending [52,53]. The amide I band is considered as more sensitive for understanding the changes in the secondary structures of proteins [54,55] and the ␣-helical contents of the proteins give the particular absorption at wavelengths which are ranging from 1652 to 1662 cm −1 [56,57].…”
Section: Ftir Measurementsmentioning
confidence: 99%
“…Among these amide bands amide I and amide II are more important. Amide I band originates between 1600 and 1700 cm −1 and is due to the C O stretching while amide II band appears in between 1500 and 1600 cm −1 owing to the C N stretching coupled with N H bending [52,53]. The amide I band is considered as more sensitive for understanding the changes in the secondary structures of proteins [54,55] and the ␣-helical contents of the proteins give the particular absorption at wavelengths which are ranging from 1652 to 1662 cm −1 [56,57].…”
Section: Ftir Measurementsmentioning
confidence: 99%
“…Obviously, the increase of the number of highly movable protons is not directly related to the amount of the sorbed organic sol- vent but is closely connected with the actual protein conformation. We have deduced previously from FTIR measurements [18,25] that the excess helicity in dry HSA samples immersed in anhydrous solvents is produced at the expense of unordered and 13-structured parts of the backbone, including those from interprotein contacts. We come to the conclusion that the disruption of interprotein contacts and increase of the backbone helicity could result in a less tight packing, facilitating less constrained liquidlike motion of some part of the side chain groups.…”
Section: The Reasons Of the Increased Mobility In Acetonitrilementioning
confidence: 99%
“…Infrared spectra of proteins exhibit a number of the amide bands, which represent different vibrations of the peptide moiety. Among the amide bands of the protein, amide I band ranging from 1600 to 1700 cm À 1 (mainly CQO stretch) and amide II band E 1548 cm À 1 (C-N stretch coupled with N-H bending mode) have been widely accepted as the typical ones to be used [32]. As shown in Fig.…”
Section: Synchronous Fluorescence Uv-vis CD and Ft-ir Spectramentioning
confidence: 99%