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DYNAMIC SURFACE ELASTICITY OF Β-CASEIN SOLUTIONS DURING ADSORPTION. / Noskovy, B.A.; Latnikova, A.V.; Lin, S.-Y.; Loglio, G.; Miller, R.

In: Journal of Physical Chemistry C, No. 45, 2007, p. 16895-16901.

Research output: Contribution to journalArticlepeer-review

Harvard

Noskovy, BA, Latnikova, AV, Lin, S-Y, Loglio, G & Miller, R 2007, 'DYNAMIC SURFACE ELASTICITY OF Β-CASEIN SOLUTIONS DURING ADSORPTION', Journal of Physical Chemistry C, no. 45, pp. 16895-16901. <http://elibrary.ru/item.asp?id=12025639>

APA

Noskovy, B. A., Latnikova, A. V., Lin, S-Y., Loglio, G., & Miller, R. (2007). DYNAMIC SURFACE ELASTICITY OF Β-CASEIN SOLUTIONS DURING ADSORPTION. Journal of Physical Chemistry C, (45), 16895-16901. http://elibrary.ru/item.asp?id=12025639

Vancouver

Noskovy BA, Latnikova AV, Lin S-Y, Loglio G, Miller R. DYNAMIC SURFACE ELASTICITY OF Β-CASEIN SOLUTIONS DURING ADSORPTION. Journal of Physical Chemistry C. 2007;(45):16895-16901.

Author

Noskovy, B.A. ; Latnikova, A.V. ; Lin, S.-Y. ; Loglio, G. ; Miller, R. / DYNAMIC SURFACE ELASTICITY OF Β-CASEIN SOLUTIONS DURING ADSORPTION. In: Journal of Physical Chemistry C. 2007 ; No. 45. pp. 16895-16901.

BibTeX

@article{f3fae57e49884a55bc330d582af547a8,
title = "DYNAMIC SURFACE ELASTICITY OF Β-CASEIN SOLUTIONS DURING ADSORPTION",
abstract = "The nonmonotonic kinetic dependencies of the dynamic elasticity of adsorbed and spread β-casein layers at the liquid-gas interface have been determined by the oscillating barrier method. While two local maxima in the surface elasticity versus concentration dependence are well documented in literature, these features have not been reported for kinetic curve. The surface elasticity in the time range of the second maximum depended on the β-casein bulk concentration and deviated from the elasticity of spread β-casein layers at the same surface pressures. In parallel to the surface viscoelasticity of PEO-PPO-PEO block copolymers, the experimental findings for β-casein can be explained by a separation of relatively hydrophobic groups of the polypeptide chain during the slow process of protein adsorption. {\textcopyright} 2007 American Chemical Society.",
author = "B.A. Noskovy and A.V. Latnikova and S.-Y. Lin and G. Loglio and R. Miller",
year = "2007",
language = "English",
pages = "16895--16901",
journal = "Journal of Physical Chemistry C",
issn = "1932-7447",
publisher = "American Chemical Society",
number = "45",

}

RIS

TY - JOUR

T1 - DYNAMIC SURFACE ELASTICITY OF Β-CASEIN SOLUTIONS DURING ADSORPTION

AU - Noskovy, B.A.

AU - Latnikova, A.V.

AU - Lin, S.-Y.

AU - Loglio, G.

AU - Miller, R.

PY - 2007

Y1 - 2007

N2 - The nonmonotonic kinetic dependencies of the dynamic elasticity of adsorbed and spread β-casein layers at the liquid-gas interface have been determined by the oscillating barrier method. While two local maxima in the surface elasticity versus concentration dependence are well documented in literature, these features have not been reported for kinetic curve. The surface elasticity in the time range of the second maximum depended on the β-casein bulk concentration and deviated from the elasticity of spread β-casein layers at the same surface pressures. In parallel to the surface viscoelasticity of PEO-PPO-PEO block copolymers, the experimental findings for β-casein can be explained by a separation of relatively hydrophobic groups of the polypeptide chain during the slow process of protein adsorption. © 2007 American Chemical Society.

AB - The nonmonotonic kinetic dependencies of the dynamic elasticity of adsorbed and spread β-casein layers at the liquid-gas interface have been determined by the oscillating barrier method. While two local maxima in the surface elasticity versus concentration dependence are well documented in literature, these features have not been reported for kinetic curve. The surface elasticity in the time range of the second maximum depended on the β-casein bulk concentration and deviated from the elasticity of spread β-casein layers at the same surface pressures. In parallel to the surface viscoelasticity of PEO-PPO-PEO block copolymers, the experimental findings for β-casein can be explained by a separation of relatively hydrophobic groups of the polypeptide chain during the slow process of protein adsorption. © 2007 American Chemical Society.

M3 - Article

SP - 16895

EP - 16901

JO - Journal of Physical Chemistry C

JF - Journal of Physical Chemistry C

SN - 1932-7447

IS - 45

ER -

ID: 5039334