Optical absorption spectra of deoxy- and oxyhemoglobin in the temperature range 300—20 K: Relation with protein dynamics
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2020, Enzyme and Microbial TechnologyCitation Excerpt :It is very important to account for the temperature effect on the extinction coefficients and obtaining accurate values of the concentration from measurements of optical absorbance [21]. For example, a decrease in temperature from 25 to −73 °C increased the εdeoxyhemoglobin at 758 nm by ∼0.22 mM−1 cm−1 [31]. At HHP, the production of oxidized o-dianisidine using native, aniline-, or benzoate-modified GOx was faster compared to atmospheric pressure at the corresponding temperature.
Second derivative analysis of synthesized spectra for resolution and identification of overlapped absorption bands of amino acid residues in proteins: Bromelain and ficin spectra in the 240–320 nm range
2020, Spectrochimica Acta - Part A: Molecular and Biomolecular SpectroscopyCitation Excerpt :A significant progress in study of biomacromolecules under the action of various physico-chemical factors can be achieved combining the protein spectral data with the experimental structure analysis together with the analytic and numeric calculation method [19–27]. In particular, some important changes in a macromolecule (or its components) caused by a number of physico-chemical factors can be traced in the protein absorption spectra recorded for studying the structural and functional properties of biopolymers [28–35]. Although the molecular absorption spectroscopy offers such analytical advantages as non-destructive real-time control, this method is characterized by a limited selectivity [36–41] which complicates analysis of multi-component systems including proteins and their complexes.
Raman spectroscopic discrimination of normal and cancerous lung tissues
2019, Spectrochimica Acta - Part A: Molecular and Biomolecular SpectroscopyCitation Excerpt :Spectral difference between normal and abnormal lung tissues should be described in terms of the following changes in composition and structure of biomolecules: (i) the ratio between lipid and protein marker bands, (ii) compositional and conformational changes in proteins including the contribution of collagen, and (iii) impact of other biomolecules (nucleic acids, polysaccharides, small molecules etc.). Negative bands of difference FT-Raman spectrum at 1207 cm−1 (C-Ph stretching), 1376 and 1332 cm−1 (Trp doublet), 1041 and 1010 cm−1 (Phe), 877 cm−1 (Trp), 858 and 831 cm−1 (Tyr doublet), 755 cm−1 (Trp) arose from vibrations of aromatic amino acids [44–46]. Several positive bands at 1629–1578 cm−1 have contribution of CC stretching vibrations in aromatics including aromatic amino acids [44–46] and reminder Hb [29–31].
Infrared absorption study of the heme pocket dynamics of carbonmonoxyheme proteins
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