The Stability Curve of Hen Egg White Lysozyme

Saronya   S.   Younvanich; B.      Mark Britt

doi:10.2174/092986606777841163

Abstract

The physiological stability curve -- a plot of the free energy of unfolding versus temperature -- is calculated for hen egg white lysozyme from a combination of extrapolated unfolding thermodynamic data from reversible conditions and isothermal titrations with guanidine hydrochloride. The shape of the curve suggests the existence of only one folded conformation.

Keywords: differential scanning calorimetry (DSC), protein stability, Titration, Gibbs-Helmholtz equation, lysozyme stability, guanidine hydrochloride

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Protein & Peptide Letters

Title: The Stability Curve of Hen Egg White Lysozyme

Volume: 13 Issue: 8

Author(s): Saronya S. Younvanich and B. Mark Britt

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Keywords: differential scanning calorimetry (DSC), protein stability, Titration, Gibbs-Helmholtz equation, lysozyme stability, guanidine hydrochloride

Abstract: The physiological stability curve -- a plot of the free energy of unfolding versus temperature -- is calculated for hen egg white lysozyme from a combination of extrapolated unfolding thermodynamic data from reversible conditions and isothermal titrations with guanidine hydrochloride. The shape of the curve suggests the existence of only one folded conformation.

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Younvanich S. Saronya and Mark Britt B., The Stability Curve of Hen Egg White Lysozyme, Protein & Peptide Letters 2006; 13 (8) . https://dx.doi.org/10.2174/092986606777841163