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Synergetic effect of sodium polystyrene sulfonate and guanidine hydrochloride on the surface properties of lysozyme solutions. / Milyaeva, O.Y.; Campbell, R.A.; Lin, S.-Y.; Loglio, G.; Miller, R.; Tihonov, M.M.; Varga, I.; Volkova, A.V.; Noskov, B.A.

в: RSC Advances, Том 5, № 10, 2015, стр. 7413-7422.

Результаты исследований: Научные публикации в периодических изданияхстатьяРецензирование

Harvard

Milyaeva, OY, Campbell, RA, Lin, S-Y, Loglio, G, Miller, R, Tihonov, MM, Varga, I, Volkova, AV & Noskov, BA 2015, 'Synergetic effect of sodium polystyrene sulfonate and guanidine hydrochloride on the surface properties of lysozyme solutions', RSC Advances, Том. 5, № 10, стр. 7413-7422. https://doi.org/10.1039/c4ra14330b

APA

Vancouver

Author

Milyaeva, O.Y. ; Campbell, R.A. ; Lin, S.-Y. ; Loglio, G. ; Miller, R. ; Tihonov, M.M. ; Varga, I. ; Volkova, A.V. ; Noskov, B.A. / Synergetic effect of sodium polystyrene sulfonate and guanidine hydrochloride on the surface properties of lysozyme solutions. в: RSC Advances. 2015 ; Том 5, № 10. стр. 7413-7422.

BibTeX

@article{be711de4538544148bedf1e29ff1b54c,
title = "Synergetic effect of sodium polystyrene sulfonate and guanidine hydrochloride on the surface properties of lysozyme solutions",
abstract = "{\textcopyright} 2015 The Royal Society of Chemistry. A study of the dilational surface viscoelastic properties of mixed solutions of lysozyme and denaturing agents with different chemical natures allows us to characterize the changes of protein tertiary structure in the surface layer upon adsorption at the liquid-gas interface. We show that guanidine hydrochloride (GuHCl) and urea influence the dynamic surface properties of lysozyme solutions less than the properties of previously studied solutions of bovine serum albumin and β-lactoglobulin. Although the addition of sodium polystyrene sulfonate (PSS) changes the kinetic dependencies of the surface properties and leads to the formation of large aggregates in the bulk phase, the dependencies of the dynamic surface elasticity on the surface pressure almost coincide with the results for pure lysozyme solutions thereby indicating the preservation of the adsorption layer structure. At the same time, the simultaneous addition of PSS and GuHCl to lysozyme solutions results in a s",
author = "O.Y. Milyaeva and R.A. Campbell and S.-Y. Lin and G. Loglio and R. Miller and M.M. Tihonov and I. Varga and A.V. Volkova and B.A. Noskov",
year = "2015",
doi = "10.1039/c4ra14330b",
language = "English",
volume = "5",
pages = "7413--7422",
journal = "RSC Advances",
issn = "2046-2069",
publisher = "Royal Society of Chemistry",
number = "10",

}

RIS

TY - JOUR

T1 - Synergetic effect of sodium polystyrene sulfonate and guanidine hydrochloride on the surface properties of lysozyme solutions

AU - Milyaeva, O.Y.

AU - Campbell, R.A.

AU - Lin, S.-Y.

AU - Loglio, G.

AU - Miller, R.

AU - Tihonov, M.M.

AU - Varga, I.

AU - Volkova, A.V.

AU - Noskov, B.A.

PY - 2015

Y1 - 2015

N2 - © 2015 The Royal Society of Chemistry. A study of the dilational surface viscoelastic properties of mixed solutions of lysozyme and denaturing agents with different chemical natures allows us to characterize the changes of protein tertiary structure in the surface layer upon adsorption at the liquid-gas interface. We show that guanidine hydrochloride (GuHCl) and urea influence the dynamic surface properties of lysozyme solutions less than the properties of previously studied solutions of bovine serum albumin and β-lactoglobulin. Although the addition of sodium polystyrene sulfonate (PSS) changes the kinetic dependencies of the surface properties and leads to the formation of large aggregates in the bulk phase, the dependencies of the dynamic surface elasticity on the surface pressure almost coincide with the results for pure lysozyme solutions thereby indicating the preservation of the adsorption layer structure. At the same time, the simultaneous addition of PSS and GuHCl to lysozyme solutions results in a s

AB - © 2015 The Royal Society of Chemistry. A study of the dilational surface viscoelastic properties of mixed solutions of lysozyme and denaturing agents with different chemical natures allows us to characterize the changes of protein tertiary structure in the surface layer upon adsorption at the liquid-gas interface. We show that guanidine hydrochloride (GuHCl) and urea influence the dynamic surface properties of lysozyme solutions less than the properties of previously studied solutions of bovine serum albumin and β-lactoglobulin. Although the addition of sodium polystyrene sulfonate (PSS) changes the kinetic dependencies of the surface properties and leads to the formation of large aggregates in the bulk phase, the dependencies of the dynamic surface elasticity on the surface pressure almost coincide with the results for pure lysozyme solutions thereby indicating the preservation of the adsorption layer structure. At the same time, the simultaneous addition of PSS and GuHCl to lysozyme solutions results in a s

U2 - 10.1039/c4ra14330b

DO - 10.1039/c4ra14330b

M3 - Article

VL - 5

SP - 7413

EP - 7422

JO - RSC Advances

JF - RSC Advances

SN - 2046-2069

IS - 10

ER -

ID: 3931990