Segawa S, Sugihara M, Maeda T, Mitsuhisa Y, Kodama M, Seki S, Sakiyama M
Biopolymers. 1989 Jun;28(6):1033-41. doi: 10.1002/bip.360280602.
Thermodynamics of unfolding of lysozyme cross-linked between Glu 35 and Trp 108 were studied in solutions of various concentrations of 1-propanol (1-PrOH) at pH 3.7 by means of scanning microcalorimetry. The transition temperature for the cross-linked lysozyme increases by 17-19 degrees 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-1, which is independent of the concentration of 1-PrOH. 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.
通过扫描量热法研究了在pH 3.7的不同浓度1-丙醇（1-PrOH）溶液中，连接在Glu 35和Trp 108之间的溶菌酶的去折叠热力学。在每种1-PrOH浓度下，由于交联作用，交联溶菌酶的转变温度升高了17-19摄氏度。这相当于去折叠吉布斯自由能增加了约28 kJ·mol-1，且该值与1-PrOH的浓度无关。研究发现，如果在相同温度下比较，交联溶菌酶的去折叠焓仅比完整溶菌酶略大，而交联溶菌酶的去折叠熵几乎与完整溶菌酶相等。基于这些量热数据讨论了交联溶菌酶的稳定机制。
