Effect of the air-water interface on the stability of β-lactoglobulin

被引：53
|
作者：
Perriman, Adam W.
Henderson, Mark J.
Holt, Stephen A.
White, John W. [1 ]
机构：
[1] Australian Natl Univ, Res Sch Chem, Canberra, ACT 0200, Australia
[2] CCLRC Rutherford Appleton Lab, ISIS, Didcot OX11 0QX, Oxon, England
来源：
JOURNAL OF PHYSICAL CHEMISTRY B | 2007年 / 111卷 / 48期
关键词：
D O I：
10.1021/jp074777r
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：
We report the X-ray and neutron reflectometry measurements of the structural changes caused by chemical denaturation of a surface excess of the bovine milk protein, beta-lactoglobulin. The thickness of the diffuse protein surface layer was used as an order parameter as there was no corresponding increase in the surface excess as a function of guanidinium chloride (G.HCl) concentration. A thermodynamic analysis performed gave the interfacial free energy of unfolding in the absence of a denaturant (Delta G(0)). This energy, lower than the free energy of unfolding bulk solution, shows that the air-water interface has a destabilizing effect on protein structure up to 50 kJ mol(-1).
引用
收藏
页码：13527 / 13537
页数：11
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