217
8 Two-Dimensional Mid-Infrared Correlation Spectroscopy in Protein Research
troscopy methods: mid-IR [36–89], near-IR [36, 38, 90–99], vibrational circular
dichroism (vCd) [43, 100, 101], electronic circular dichroism (ECd) [41, 102],
Raman [40, 41, 103–107], Raman optical activity (RoA) [105, 107–111], deep uv
resonance Raman (duvRR) [28, 31, 32, 112–114], and fluorescence [115–118].
most of these applications use mid-infrared spectroscopy, and this use explains the
general popularity of this method in the investigation of different quantitative problems in biomolecular systems.
A few reviews devoted to the application of Raman, near- and mid-IR 2dCoS to
protein research were given in [32, 119–121] along with detailed descriptions of the
background and of the computational procedures. Additionally, in chapter 12 in the
text book [1], the authors focus on infrared 2dCoS as a powerful tool in the examination of three selected protein systems. the most recent review of the application
of vibrational 2DCoS to biological compounds was provided by Ozaki and Šašic
[122] where results from [52] were presented in detail.
8.3.1 Pretreatment stage of 2DCoS analysis
measurements as a function of the different perturbations listed in Fig. 8.1 do not
require advanced equipment and can be conducted on an ordinary commercial IR
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8 Two-Dimensional Mid-Infrared Correlation Spectroscopy in Protein Research
troscopy methods: mid-IR [36–89], near-IR [36, 38, 90–99], vibrational circular
dichroism (vCd) [43, 100, 101], electronic circular dichroism (ECd) [41, 102],
Raman [40, 41, 103–107], Raman optical activity (RoA) [105, 107–111], deep uv
resonance Raman (duvRR) [28, 31, 32, 112–114], and fluorescence [115–118].
most of these applications use mid-infrared spectroscopy, and this use explains the
general popularity of this method in the investigation of different quantitative problems in biomolecular systems.
A few reviews devoted to the application of Raman, near- and mid-IR 2dCoS to
protein research were given in [32, 119–121] along with detailed descriptions of the
background and of the computational procedures. Additionally, in chapter 12 in the
text book [1], the authors focus on infrared 2dCoS as a powerful tool in the examination of three selected protein systems. the most recent review of the application
of vibrational 2DCoS to biological compounds was provided by Ozaki and Šašic
[122] where results from [52] were presented in detail.
8.3.1 Pretreatment stage of 2DCoS analysis
measurements as a function of the different perturbations listed in Fig. 8.1 do not
require advanced equipment and can be conducted on an ordinary commercial IR
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