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Raman Spectroscopy: Overview01:20

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The underlying principle of Raman spectroscopy is based on the interaction between light and matter, specifically molecules' inelastic scattering of photons. When a monochromatic beam of light, typically from a laser source, interacts with a sample, most scattered light has the same frequency as the incident light. This is known as Rayleigh scattering.
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The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
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At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
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It is essential to understand the difference between chiral and achiral interactions and the implications thereof in optical activity and their applications. Just as our feet, which are chiral, interact uniquely with chiral objects, such as a pair of shoes, but identically with achiral socks, enantiomers of a molecule exhibit different properties only when they interact with other chiral media. An example of a significant implication from this facet is the phenomenon known as optical activity,...
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A conventional Raman spectrophotometer includes a laser source, a sample holding system, a wavelength selector, and a detector.
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Selective DMSO-induced conformational changes in proteins from Raman optical activity.

Andrea N L Batista1, João M Batista, Vanderlan S Bolzani

  • 1Manchester Institute of Biotechnology and Faculty of Life Sciences, University of Manchester, 131 Princess street, Manchester M1 7DN, UK. e.blanch@manchester.ac.uk joaombj@hotmail.com.

Physical Chemistry Chemical Physics : PCCP
|October 29, 2013
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Dimethyl sulfoxide (DMSO) completely destabilizes protein alpha-helices into PPII helix structures at high concentrations. However, beta-sheets remain largely unaffected by DMSO, regardless of concentration.

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Area of Science:

  • Biochemistry
  • Spectroscopy
  • Structural Biology

Background:

  • Protein function is dictated by its structure, which is influenced by the surrounding solvent environment.
  • The role of non-aqueous solvents, specifically dimethyl sulfoxide (DMSO), in protein structure regulation is a subject of ongoing scientific discussion.

Purpose of the Study:

  • To conclusively investigate the effects of DMSO on the secondary structure of various proteins using Raman and Raman optical activity (ROA) spectroscopies.
  • To elucidate the conformational changes induced by different concentrations of DMSO in proteins with diverse secondary structure compositions.

Main Methods:

  • Utilized Raman and Raman optical activity (ROA) spectroscopies to analyze protein secondary structure.
  • Examined a range of proteins: human serum albumin, bovine α-lactalbumin, bovine ribonuclease A, bovine β-lactoglobulin, and bovine α-casein.
  • Tested protein samples in varying concentrations of DMSO, including 100% and 10% (v/v).

Main Results:

  • 100% DMSO solutions completely destabilized α-helices, converting them to the poly(L-proline) II (PPII) helix conformation.
  • Low DMSO concentrations (10% v/v) had minimal impact on the secondary structure of even highly helical proteins.
  • β-sheets were largely unaffected by DMSO across all tested concentrations.
  • The natively unfolded protein, α-casein, became further disordered in pure DMSO.

Conclusions:

  • DMSO significantly alters protein secondary structure, specifically destabilizing α-helices into PPII conformations.
  • Vibrational optical activity (VOA) techniques are highly effective for assessing biomolecular conformations in non-traditional environments like organic solvents.
  • Findings provide crucial insights into protein behavior in organic solvents, expanding structural biology's reach beyond traditional methods like X-ray crystallography and NMR.