@article {Younvanich:2006:0929-8665:769,
title = "The Stability Curve of Hen Egg White Lysozyme",
journal = "Protein and Peptide Letters",
parent_itemid = "infobike://ben/ppl",
publishercode ="ben",
year = "2006",
volume = "13",
number = "8",
publication date ="2006-08-01T00:00:00",
pages = "769-772",
itemtype = "ARTICLE",
issn = "0929-8665",
url = "https://www.ingentaconnect.com/content/ben/ppl/2006/00000013/00000008/art00003",
doi = "doi:10.2174/092986606777841163",
keyword = "Titration, guanidine hydrochloride, differential scanning calorimetry (DSC), protein stability, Gibbs-Helmholtz equation, lysozyme stability",
author = "Younvanich, Saronya S. and Mark Britt, B.",
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. ",
}