| Circular dichroism spectral studies on the recombinant human neuroglobin |
| |
| 作者姓名： | ZHAO Chao LI Lianzhi WANG Li JI Haiwei |
| |
| 作者单位： | [1]School of Chemistry and Chemical Engineering, Liaocheng University,Liaocheng 252059, China [2]State Key-Laboratory of Coordination Chemistry, Nanjing University,Nanjing 210093, China |
| |
| 基金项目： | Acknoledgements We thank Prof. Burmester T., Johannes Gutenberg University of Mainz, Germany, for kindly providing the gene of neuroglobin and Prof. Guo Zijian of State Key Laboratory of Coordination Chemistry, Nanjing University, for the great support and help. This work was supported by the National Natural Science Foundation of China （Grant No. 20471025）. |
| |
| 摘 要： | Neuroglobin (NGB) is a newly discov- ered member of the hemoglobin superfamily that is primarily expressed in the brain of humans and other vertebrates. The effects of protein concentration, solvent, pH and temperature on the secondary structure of NGB were investigated by employing far UV circular dichroism (CD) spectroscopy. The results show that NGB exists mainly in α-helix form when its concentration is less than 10 μmol/L. However, its α-helix content decreases with the increase of con- centration in the range of 10―40 μmol/L and remains unchanged when the concentration is higher than 40 μmol/L, which suggest that NGBs form intermolecular disulfide bond and aggregate in higher concentration. The α-helix content of NGB in methanol and ethanol is a little higher than that in water, indicating a higher stability of NGB in these solvents. NGB loses its α-helical secondary structure in either acidic or alka- line solution to some extent. Although increased temperature destabilizes the α-helices of NGB, over 16% of α-helices can be kept at 110°C. Therefore, NGB is a protein with hyperthermal stability.
|
| 关 键 词： | 血红蛋白 脊椎动物 CD光谱 二级结构 稳定性 |
| 文章编号： | 10.1007/s11434-006-2144-7 |
| 收稿时间： | 2006-03-16 |
| 修稿时间： | 2006-03-162006-05-26 |
Circular dichroism spectral studies on the recombinant human neuroglobin |
| |
| ZHAO Chao LI Lianzhi WANG Li JI Haiwei.Circular dichroism spectral studies on the recombinant human neuroglobin[J].Chinese Science Bulletin,2006,51(21):2581-2585. |
| |
| Authors: | Chao Zhao Lianzhi Li Li Wang Haiwei Ji |
| |
| Institution: | (1) School of Chemistry and Chemical Engineering, Liaocheng University, Liaocheng, 252059, China;(2) State Key Laboratory of Coordination Chemistry, Nanjing University, Nanjing, 210093, China |
| |
| Abstract: | Neuroglobin (NGB) is a newly discovered member of the hemoglobin superfamily that is primarily expressed in the brain of humans
and other vertebrates. The effects of protein concentration, solvent, pH and temperature on the secondary structure of NGB
were investigated by employing far UV circular dichroism (CD) spectroscopy. The results show that NGB exists mainly in α-helix
form when its concentration is less than 10 μmol/L. However, its α-helix content decreaes with the increase of concentration
in the range of 10–40 μmol/L and remains unchanged when the concentration is higher than 40 μmol/L, which suggest that NGBs
form intermolecular disulfide bond and aggregate in higher concentration. The α-helix content of NGB in methanol and ethanol
is a little higher than that in water, indicating a higher stability of NGB in these solvents. NGB loses its α-helical secondary
structure in either acidic or alkaline solution to some extent. Although increased temperature destabilizes the α-helices
of NGB, over 16% of α-helices can be kept at 110°C. Therefore, NGB is a protein with hyperthermal stability. |
| |
| Keywords: | neuroglobin CD spectra secondary structure stability |
| 本文献已被 CNKI 维普 万方数据 SpringerLink 等数据库收录！ |
| 点击此处可从《中国科学通报(英文版)》浏览原始摘要信息 |
| 点击此处可从《中国科学通报(英文版)》下载免费的PDF全文 |
