摘要
在不同操作电压和温度下,SDS-蛋白质在无胶筛分电泳的实验结果表明,电泳力学迁移模型(EMMM)比传统经验式更能准确地反映实验事实.SDS-蛋白质对构象参数(Rc)随热力学温度增加而变化,在288—298K范围内Rc迅速变小,而在298~313K范围内,温度变化对其影响不大.不同的SDS-蛋白质在一定条件下具有相近的活化能,该结论进一步从热力学方面支持了EMMM的一个基本结论,即不同相对分子质量Mr的SDS-蛋白质在同一NGS实验条件下具有相似的形状或构象,并与SDS-蛋白质分子为长棒状这一客观事实相符合.
With different operating voltages and temperatures, experiments of SDS proteins on the nongelsieve electrophoresis clearly depict that EMMM refects the experimental facts more accurately than is possible with the traditional empirical models. The relative conformation parameters of SDS-proteins change with the incresse in temperature. It decreases rapidly within the range 288 ̄298K. But within 298 ̄313K,temperature changes do not affect it too much. Under the Same condition, different SDSproteins have nearly the same active energy. Thermodynamically, this conclusion supports one of the basic infermas, namely that different macromolecule SDS-proteins have similar shape or conformation in the same NGS experiment condition. It is in accord with the objective fact that SDS-proteins exist in the form of long protraced stretches.
出处
《北京理工大学学报》
EI
CAS
CSCD
1996年第2期186-190,共5页
Transactions of Beijing Institute of Technology
基金
高等学校博士点专项研究基金