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

Adam W. Perriman; Mark J. Henderson; Stephen A. Holt; John W. White

doi:10.1021/jp074777r

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

Adam W. Perriman, Mark J. Henderson, Stephen A. Holt, John W. White^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

55 Citations (Scopus)

Abstract

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, β-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 (ΔG⁰). 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.

Original language	English
Pages (from-to)	13527-13537
Number of pages	11
Journal	Journal of Physical Chemistry B
Volume	111
Issue number	48
DOIs	https://doi.org/10.1021/jp074777r
Publication status	Published - 6 Dec 2007

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abstract = "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, β-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 (ΔG0). 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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AU - Perriman, Adam W.

AU - Henderson, Mark J.

AU - Holt, Stephen A.

AU - White, John W.

PY - 2007/12/6

Y1 - 2007/12/6

N2 - 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, β-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 (ΔG0). 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.

AB - 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, β-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 (ΔG0). 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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DO - 10.1021/jp074777r

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JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

IS - 48

ER -

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

Abstract

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