The Stability Curve of Hen Egg White Lysozyme

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

Document Type: Research Article


Affiliations: Department of Chemistry and Physics, Texas Woman's University, Denton, TX 76204 USA.

Publication date: August 1, 2006

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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