Impact of Globule Unfolding on Dilational Viscoelasticity of β-Lactoglobulin Adsorption Layers

被引：48
|
作者：
Noskov, B. A. [1 ]
Grigoriev, D. O. [2 ]
Latnikova, A. V. [1 ]
Lin, S. -Y. [3 ]
Loglio, G. [4 ]
Miller, R. [2 ]
机构：
[1] St Petersburg State Univ, Fac Chem, St Petersburg 198904, Russia
[2] MPI Kolloid & Grenzflachenforsch, D-14476 Golm, Germany
[3] Natl Taiwan Univ Sci & Technol, Dept Chem Engn, Taipei 106, Taiwan
[4] Univ Florence, Dipartimento Chim Organ, I-50019 Florence, Italy
来源：
JOURNAL OF PHYSICAL CHEMISTRY B | 2009年 / 113卷 / 40期
关键词：
AIR-WATER-INTERFACE; DYNAMIC SURFACE-PROPERTIES; AIR/WATER INTERFACE; STRUCTURAL CONFORMATION; LIQUID INTERFACES; NEUTRON REFLECTION; PROTEIN ADSORPTION; POLYMER-SOLUTIONS; LYSOZYME LAYERS; FILM FORMATION;
D O I：
10.1021/jp905413q
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
The dynamic surface dilational elasticity, surface Pressure, and adsorbed amount of the mixed solutions Of beta-lactoglobulin and guanidine hydrochloride were measured as a function of surface age and denaturant concentration. It was shown that the conformational transition from compact globules to disordered protein molecules ill the surface layer leads to strong changes in the surface elasticity kinetic dependencies and thereby can be easily detected by measuring the surface dilational rheological properties. The corresponding changes of the kinetic dependencies of the surface pressure and adsorbed amount are not so pronounced but correlate with the results on Surface dilational elasticity.
引用
收藏
页码：13398 / 13404
页数：7
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