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The Chemical Educator
ISSN: 1430-4171 (electronic version)
Abstract Volume 13
Issue 1 (2008) pp 16-18
Thermal Unfolding of Lysozyme Studied by UV Difference Spectroscopy
Salvador R. Tello-Solís
Departamento de Química. Universidad Autónoma Metropolitana-Iztapalapa,
P.O. Box 55-534, Iztapalapa, D.F., 09340, México,
srts@xanum.uam.mx
Received March 12, 2007. Accepted August 11, 2007.
Published online: 1 February 2008
Abstract. This laboratory experience describes an experiment for the study of the thermal stability of a protein, lysozyme, using UV difference spectroscopy. The van’t Hoff enthalpy of thermal unfolding, DH°U, of lysozyme was determined from direct estimation of the equilibrium constant at several temperatures (DH°U = 521 kJ/mol). This experiment is appropriate for undergraduate biochemistry or biophysical chemistry course in which the thermal stability of a protein should be emphasized.
Key Words: Laboratories and Demonstrations; physical chemistry; thermal denaturation; UV difference spectroscopy; protein; lysozyme
(*) Corresponding author. (E-mail: srts@xanum.uam.mx)
Article in PDF format (103 KB) HTML format
Issue date: February
1, 2008
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