蛋白质溶液可逆热变性及其与肽链构象关系的研究  

STUDIES ON THE REVERSIBILITY OF THERMODENATURATION IN PROTEIN SOLUTION AND THE RELATION WTIH CONFORMATION OF PRPITDE CHAIN

作　　者：傅亚珍[1] 

机构地区：[1]中国科学院生物物理研究所

出　　处：《生物物理学报》1994年第1期1-5,共5页Acta Biophysica Sinica

基　　金：国家自然科学基金

摘　　要：用微量扫描量热技术及远紫外圆二色谱研究了蛋白质水溶液的浓度和ｐＨ对蛋白质热变性可逆性的影响及其与在热变性时肽链构象的关系。结果表明，当蛋白质溶液的浓度为０．０４％、ｐＨ为３时可实现完全可逆的热变性，然而蛋白质溶液宏观上的热变性并不意味着微观上蛋白质分子肽链的完全伸展。The effect of PH and protein concentxation in solution on revereibility ofthennodenaurtion and the relation with confonnation of peptide chain at thennaldenauration state were studied by differential scanning caloimeter and cellular dichroism Theadults shoal that thennodenaturation in the proals solution (concentration is 0.04% and pHis 3) wu completely reversible, but the thennodenatulation in macroscopic vieW did not meantotal. unfolding of peptide chain in ndroscopic view.

关 键 词：热变性 肽链 构象 蛋白 

分 类 号：Q71[生物学—分子生物学] Q510.1