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).

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收藏

页码：13527 / 13537

页数：11

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