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Issue 42, 2014
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Collective hydration dynamics of guanidinium chloride solutions and its possible role in protein denaturation: a terahertz spectroscopic study

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Abstract

The remarkable ability of guanidinium chloride (GdmCl) to denature proteins is a well studied yet controversial phenomenon; the exact molecular mechanism is still debatable, especially the role of hydration dynamics, which has been paid less attention. In the present contribution, we have addressed the issue of whether the collective hydrogen bond dynamics of water gets perturbed in the presence of GdmCl and its possible impact on the denaturation of a globular protein human serum albumin (HSA), using terahertz (THz) time domain spectroscopy (TTDS) in the frequency range of 0.3–2.0 THz. The collective hydrogen bond dynamics is determined by fitting the obtained complex dielectric response in a multiple Debye relaxation model. To compare the results, the studies were extended to two more salts: tetramethylguanidinium chloride (TMGdmCl) and sodium chloride (NaCl). It was concluded that the change in hydration dynamics plays a definite role in the protein denaturation process.

Graphical abstract: Collective hydration dynamics of guanidinium chloride solutions and its possible role in protein denaturation: a terahertz spectroscopic study

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Publication details

The article was received on 23 Jul 2014, accepted on 08 Sep 2014 and first published on 09 Sep 2014


Article type: Paper
DOI: 10.1039/C4CP03273J
Phys. Chem. Chem. Phys., 2014,16, 23308-23315

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    Collective hydration dynamics of guanidinium chloride solutions and its possible role in protein denaturation: a terahertz spectroscopic study

    N. Samanta, D. D. Mahanta and R. K. Mitra, Phys. Chem. Chem. Phys., 2014, 16, 23308
    DOI: 10.1039/C4CP03273J

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