%0 Journal Article
%T THE ROLE OF WATER IN STABILIZING THE NATURAL STRUCTURE OF MYOGLOBIN-A FOURIER TRANSFORM INFRARED SPECTROSCOPIC STUDY<br>水在稳定肌红蛋白天然结构中的作用
%A Zhang Jizhen
%A Liang Qi
%A <br>张极震
%A 梁圻
%J 生物物理学报
%D 1995
%I 
%X The effects of water on the secondary structure of myoglobin was investigated in the relative huminity (RH) range of 0 to 100% by means of Fourier transform infrared spectroscopy and curve-fitting. At dryness, the relative contents of a-helix, extended and disordered structures are about 61%, 22% and 17%, respectively. As the degree of hydration increases, the content of disordered structure decreases and those of ordered secondary sturcture increase. Such a structure transition is most significant at the RH lower than 44% and a complicated interchange of disordered to ordered structure takes place at 86 to 100%RH, Where the relative contents of the three substructures are 75%, 21% and 4%, respectively, the same as those in crystal and solution. The results confirm our previous conclusion that water acts as a plasticizer for the flexibility and a catalyst for mobility and conformation of peptide chains.
%K Myogobin
%K Hydration
%K Secondar
%K structure
%K FTIR<br>肌红蛋白
%K 水合
%K 二级结构
%K 红外光谱
%K 蛋白
%K 结构
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=8760C2861E15B2FE042D7EDF145FF243&yid=BBCD5003575B2B5F&vid=708DD6B15D2464E8&iid=CA4FD0336C81A37A&sid=94C357A881DFC066&eid=F3090AE9B60B7ED1&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=4&reference_num=5