Fourier-transform infrared spectroscopy (FTIR) was used to characterize the protein and lipid content of REVs based on the specific vibrations of these molecules24 (link),31 (link). FTIR measurements were carried out using a Varian 2000 spectrometer (Scimitar Series, USA), fitted with a diamond attenuated total reflection cell (‘Golden Gate’ single reflection ATR unit, Specac, United Kingdom). Approximately 5 μl of the sample was pipetted onto the diamond ATR surface and a thin dry film was obtained by slowly evaporating the solvent under ambient conditions (approx. 10 min). Typically, 64 scans were collected at a nominal resolution of 2 cm−1. ATR correction, buffer background spectral subtraction and other spectral evaluations were performed with the Grams/32 software package (Galactic Inc., USA).
Golden gate single reflection atr unit
Manufactured by Specac
Sourced in United Kingdom
The Golden Gate' single reflection ATR unit is a compact and versatile accessory designed for Fourier Transform Infrared (FTIR) spectroscopy. It provides a simple and efficient method for analyzing the surface composition of solid or liquid samples. The unit features a diamond internal reflection element that allows for direct contact with the sample, enabling quick and easy analysis without complex sample preparation.
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5 protocols using golden gate single reflection atr unit
1
FTIR Characterization of REV Proteins and Lipids
2
ATR-FTIR Characterization of SSL Suspensions
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For FTIR spectroscopic study, the attenuated total reflection (ATR) technique was used, having a penetration depth of infrared light in the samples in the order of one micrometer, so the investigation in bulk aqueous phase was possible, too.
ATR-FTIR spectroscopic measurements were carried out by means of a Varian 2000 (Scimitar Series) FTIR spectrometer fitted with a diamond attenuated total reflection cell (Specac's “Golden Gate” single reflection ATR unit with active area of 600 × 600 μm2). SSLT (or SSL) suspension (5 μl) was spread onto the diamond ATR surface. Room temperature spectra (128 scans, resolution of 2 cm−1) were recorded both as suspension using a cap to avoid sample drying and as dry films after slow evaporation of the buffer solvent under ambient conditions. ATR correction was executed after each data collection. All spectral manipulations were performed using GRAMS/32 software package (Galactic Industries Incorporation, USA).
ATR-FTIR spectroscopic measurements were carried out by means of a Varian 2000 (Scimitar Series) FTIR spectrometer fitted with a diamond attenuated total reflection cell (Specac's “Golden Gate” single reflection ATR unit with active area of 600 × 600 μm2). SSLT (or SSL) suspension (5 μl) was spread onto the diamond ATR surface. Room temperature spectra (128 scans, resolution of 2 cm−1) were recorded both as suspension using a cap to avoid sample drying and as dry films after slow evaporation of the buffer solvent under ambient conditions. ATR correction was executed after each data collection. All spectral manipulations were performed using GRAMS/32 software package (Galactic Industries Incorporation, USA).
3
FT-IR Spectroscopic Analysis of Thin Films
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FT-IR spectroscopic measurements were carried out by means of a FT-IR spectrometer (Varian 2000, Scimitar Series, United States), fitted with a diamond attenuated total reflection cell ('Golden Gate' single reflection ATR unit with active area of 600 x 600 µm 2 , Specac, United Kingdom). 5 µl of sample was spread onto the diamond ATR surface and a thin dry film was obtained by slowly evaporating the solvent under ambient conditions (~approx. 5 min). The second derivatives of the measured spectra were obtained by the Savitsky-Golay method (third order polynomial, 5 smoothing points).
For temperature controlled measurements a home-made liquid cell with volatile solvent cover was applied; the temperature was equilibrated for 5 min before collection of each spectrum. Typically, 64 scans were collected at a nominal resolution of 2 cm -1 . After each data acquisition, ATR correction (and water background spectral subtraction) was performed. The actual frequencies of complex IR bands were determined by fitting their peaks with Lorentzian curves. For all spectral manipulation the Grams/32 software package (Galactic Inc., USA) was used.
For temperature controlled measurements a home-made liquid cell with volatile solvent cover was applied; the temperature was equilibrated for 5 min before collection of each spectrum. Typically, 64 scans were collected at a nominal resolution of 2 cm -1 . After each data acquisition, ATR correction (and water background spectral subtraction) was performed. The actual frequencies of complex IR bands were determined by fitting their peaks with Lorentzian curves. For all spectral manipulation the Grams/32 software package (Galactic Inc., USA) was used.
4
FTIR Analysis of Dried Samples
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The FTIR spectra of the samples were obtained using a PerkinElmer Spectrum 100, coupled to an ATR single-reflection Golden Gate unit (Graseby Specac LTD, Kent, UK) and a triglycine sulfate detector. All the spectra were obtained with an average of 16 scans and a scanning resolution of 4.0 cm−1. Samples were dried in a desiccator for 1 week before the tests. All the spectra were normalized against the peak at 917 cm−1, which is assigned as the skeletal stretching [37 (link)].
5
FT-IR Analysis of Protein Secondary Structure
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The FT-IR spectra were obtained using a PerkinElmer Spectrum 100, an ATR single-reflection Golden Gate unit (Graseby Specac LTD, England), and a triglycine sulfate detector. The scanning resolution was 4.0 cm–1 and the spectrum was obtained based on 32 consecutive scans. The peak deconvolution of the protein amide I region (1700–1580 cm–1) was performed as previously described by Cho et al2 (link). using the PerkinElmer Spectrum software (version 10.5.1), setting the enhancement factor (γ) and a smoothing filter to 2% and 70%, respectively. The individual protein secondary structure fractions were obtained by a Gaussian curve resolution, fitting the amide I region to 9 peaks; 1618, 1625, 1634, 1644, 1651, 1658, 1667, 1680, and 1691 cm−1. The peak centres were allowed to move ±1 cm−1 if necessary for improving the fitting result.
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