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Calorimetric study of the effect of intrachain cross-linking on lysozyme unfolding

✍ Scribed by Shin-Ichi Segawa; Mitsuru Sugihara; Tomoko Maeda; Yukio Mitsuhisa; Michiko Kodama; Syûzô Seki; Minoru Sakiyama

Publisher
Wiley (John Wiley & Sons)
Year
1989
Tongue
English
Weight
492 KB
Volume
28
Category
Article
ISSN
0006-3525

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✦ Synopsis

Synopsis

Thermodynamics of unfolding of lysozyme cross-linked between Glu 35 and Trp 108 were studied in solutions of various concentrations of l-propanol (1-F'rOH) at pH 3.7 by means of scanning microcalorimetry. The transition temperature for the cross-linked lysozyme increases by 17-19°C due to cross-linking at every concentration of 1-PrOH. This corresponds to the increase in the unfolding Gibbs free energy of about 28 kJ ' mol-', which is independent of the concentration of 1-F'rOH. It was found that the unfolding enthalpy of cross-linked lysozyme is only slightly larger than that of intact one, and the unfolding entropy of the cross-linked one is nearly equal to that of the intact one, if both are compared at the same temperature. The stabilization mechanism for the cross-linked lysozyme is discussed on the basis of these calorimetric data.

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