Nölting B
Department of Biochemistry, Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana 61801, USA.
J Theor Biol. 1995 Jul 12;175(2):191-6. doi: 10.1006/jtbi.1995.0131.
A fundamental problem in measurements of the adiabatic compressibility of macromolecules in aqueous solution using sound velocity is the unknown heat exchange between the interior of the molecule and the bulk solvent. Usually only a pseudoadiabatic compressibility is measured, which is between isothermal and adiabatic compressibility. The measured compressibility might even be close to the isothermal compressibility, depending on the experimental conditions. In this paper, a model is proposed that enables the deviation of experimental conditions from the requirement of adiabatic measurements to be estimated. This model treats the macromolecule as a heat conductive sphere. Analytical solutions for the temporal and local heat diffusion are obtained. Proteins less than 100 kDa in molecular weight at a sound frequency of less than 10 MHz are found to be essentially in thermal equilibrium with the bulk solvent. In this case, for the aqueous protein solution at temperatures < or = 25 degrees C and less than 2% protein concentration, the theory predicts that the sound velocity measurement of the interior of protein is close to isothermal conditions.
利用声速测量水溶液中大分子的绝热压缩性时,一个基本问题是分子内部与本体溶剂之间未知的热交换。通常仅测量伪绝热压缩性,其介于等温压缩性和绝热压缩性之间。根据实验条件,所测量的压缩性甚至可能接近等温压缩性。本文提出了一个模型,该模型能够估计实验条件与绝热测量要求之间的偏差。此模型将大分子视为一个导热球体。获得了时间和局部热扩散的解析解。发现在声频小于10 MHz时,分子量小于100 kDa的蛋白质基本上与本体溶剂处于热平衡状态。在这种情况下,对于温度≤25℃且蛋白质浓度小于2%的蛋白质水溶液,该理论预测蛋白质内部的声速测量接近等温条件。