Tsereteli G I, Belopol'skaia T V, Mel'nik T N
Biofizika. 1997 Jan-Feb;42(1):68-74.
The absolute values of heat capacity of the collagen-water systems with different relative content of the components in both native and denatured state were studied by the method of differential scanning calorimetry in a wide temperature range (-40 +/- 140 degrees C) which includes the region of the denaturation phase transition as well as the region of the relaxation glass transition. From the experimental data the values of denaturation increment delta Cpnd-0.42 +/- 0.04 J/(g.K) at the collagen content 10-50% and the values of glass transition increment delta Cpg-0.54 +/- 0.12 J/(g.K) for moist denatured protein were calculated. Different processes influencing the increment values are analysed. The nonequilbrium character of the glass-like state of moist proteins was clearly demonstrated in the study of glass transition.
采用差示扫描量热法,在包括变性相变区域和弛豫玻璃化转变区域的宽温度范围(-40±140℃)内,研究了天然和变性状态下具有不同组分相对含量的胶原-水体系的热容绝对值。根据实验数据,计算出胶原含量为10%-50%时的变性增量ΔCpnd-0.42±0.04 J/(g·K)以及湿变性蛋白的玻璃化转变增量ΔCpg-0.54±0.12 J/(g·K)。分析了影响增量值的不同过程。在玻璃化转变研究中,明确证明了湿蛋白类玻璃态的非平衡特性。