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Dynamic surface properties of lysozyme solutions. Impact of urea and guanidine hydrochloride. / Tihonov, M.M.; Milyaeva, O.; Noskov, B.A.

In: Colloids and Surfaces B: Biointerfaces, Vol. 129, 2015, p. 114-120.

Research output: Contribution to journal › Article

Harvard

Tihonov, MM, Milyaeva, O & Noskov, BA 2015, 'Dynamic surface properties of lysozyme solutions. Impact of urea and guanidine hydrochloride.', Colloids and Surfaces B: Biointerfaces, vol. 129, pp. 114-120. https://doi.org/10.1016/j.colsurfb.2015.03.034

APA

Tihonov, M. M., Milyaeva, O., & Noskov, B. A. (2015). Dynamic surface properties of lysozyme solutions. Impact of urea and guanidine hydrochloride. Colloids and Surfaces B: Biointerfaces, 129, 114-120. https://doi.org/10.1016/j.colsurfb.2015.03.034

Vancouver

Tihonov MM, Milyaeva O, Noskov BA. Dynamic surface properties of lysozyme solutions. Impact of urea and guanidine hydrochloride. Colloids and Surfaces B: Biointerfaces. 2015;129:114-120. https://doi.org/10.1016/j.colsurfb.2015.03.034

Author

Tihonov, M.M. ; Milyaeva, O. ; Noskov, B.A. / Dynamic surface properties of lysozyme solutions. Impact of urea and guanidine hydrochloride. In: Colloids and Surfaces B: Biointerfaces. 2015 ; Vol. 129. pp. 114-120.

BibTeX

@article{b2dd31c8e0f54e0ebff25d4c8b96e9ee,
title = "Dynamic surface properties of lysozyme solutions. Impact of urea and guanidine hydrochloride.",
abstract = "Urea and guanidine hydrochloride (GuHCl) have different influence on surface properties of lysozyme solutions. The increase of GuHCl concentration leads to noticeable changes of kinetic dependencies of the dynamic surface elasticity and ellipsometric angles while the main effect of urea reduces to a strong drop of the static surface tension. The difference between the effects of these two denaturants on the surface properties of other investigated globular proteins is significantly weaker and is mainly a consequence of a different extent of the globule unfolding in the surface layer at equal concentrations of the denaturants. The obtained results for lysozyme solutions are connected with the strongly different denaturation mechanisms under the influence of urea and GuHCl. In the former case the protein preserves its globular structure in the adsorption layer at high urea concentrations (up to 9 M) but without tightly packed interior of the globule and with a dynamic tertiary structure (molten globule state).",
author = "M.M. Tihonov and O. Milyaeva and B.A. Noskov",
year = "2015",
doi = "10.1016/j.colsurfb.2015.03.034",
language = "English",
volume = "129",
pages = "114--120",
journal = "Colloids and Surfaces B: Biointerfaces",
issn = "0927-7765",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Dynamic surface properties of lysozyme solutions. Impact of urea and guanidine hydrochloride.

AU - Tihonov, M.M.

AU - Milyaeva, O.

AU - Noskov, B.A.

PY - 2015

Y1 - 2015

N2 - Urea and guanidine hydrochloride (GuHCl) have different influence on surface properties of lysozyme solutions. The increase of GuHCl concentration leads to noticeable changes of kinetic dependencies of the dynamic surface elasticity and ellipsometric angles while the main effect of urea reduces to a strong drop of the static surface tension. The difference between the effects of these two denaturants on the surface properties of other investigated globular proteins is significantly weaker and is mainly a consequence of a different extent of the globule unfolding in the surface layer at equal concentrations of the denaturants. The obtained results for lysozyme solutions are connected with the strongly different denaturation mechanisms under the influence of urea and GuHCl. In the former case the protein preserves its globular structure in the adsorption layer at high urea concentrations (up to 9 M) but without tightly packed interior of the globule and with a dynamic tertiary structure (molten globule state).

AB - Urea and guanidine hydrochloride (GuHCl) have different influence on surface properties of lysozyme solutions. The increase of GuHCl concentration leads to noticeable changes of kinetic dependencies of the dynamic surface elasticity and ellipsometric angles while the main effect of urea reduces to a strong drop of the static surface tension. The difference between the effects of these two denaturants on the surface properties of other investigated globular proteins is significantly weaker and is mainly a consequence of a different extent of the globule unfolding in the surface layer at equal concentrations of the denaturants. The obtained results for lysozyme solutions are connected with the strongly different denaturation mechanisms under the influence of urea and GuHCl. In the former case the protein preserves its globular structure in the adsorption layer at high urea concentrations (up to 9 M) but without tightly packed interior of the globule and with a dynamic tertiary structure (molten globule state).

U2 - 10.1016/j.colsurfb.2015.03.034

DO - 10.1016/j.colsurfb.2015.03.034

M3 - Article

VL - 129

SP - 114

EP - 120

JO - Colloids and Surfaces B: Biointerfaces

JF - Colloids and Surfaces B: Biointerfaces

SN - 0927-7765

ER -

ID: 3974874