摘要
从蛋白质变性的渐变模型及构象态渐变的观点出发 ,对伸展态 β -乳球蛋白的重折叠过程进行了分析 ,发现蛋白质分子从伸展态到最终折叠态历经一系列中间稳定态 .尿素浓度梯度电泳实验结果显示 ,存在两条不同的折叠途径 .在不同的尿素浓度范围内 。
Starting from the viewpoint on sequential alternation of conformations,the refolding processes of the unfolded β lactoglobulin is analyzed.We find that the unfolded protein molecules undergo a series of steady intermediate states from unfolded conformation to the more intact conformation or native conformation.The experimental results of urea gradient electrophoresis show that there are two different refolding processes.In different regions of urea concentrations,the folding processes indicate that different processes correspond to different kinetic features.
出处
《内蒙古师范大学学报(自然科学汉文版)》
CAS
2002年第2期108-111,共4页
Journal of Inner Mongolia Normal University(Natural Science Edition)
基金
国家自然科学基金资助项目 (3996 0 0 2 3)