%0 Journal Article
%T STUDIES ON THE REVERSIBILITY OF THERMODENATURATION IN PROTEIN SOLUTION AND THE RELATION WTIH CONFORMATION OF PRPITDE CHAIN<br>蛋白质溶液可逆热变性及其与肽链构象关系的研究
%A Fu Yagi
%A <br>傅亚珍
%J 生物物理学报
%D 1994
%I 
%X 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.
%K Protein
%K Thermodenaturation
%K Conformation of peptide chain<br>蛋白质
%K 热变性
%K 肽链构象
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=7C6DDDFF97F6AD152FF9F254E37EDB1B&yid=3EBE383EEA0A6494&vid=F3090AE9B60B7ED1&iid=CA4FD0336C81A37A&sid=CA4FD0336C81A37A&eid=94C357A881DFC066&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=2&reference_num=0