Characterization of the structural and functional changes of hemoglobin in dimethyl sulfoxide by spectroscopic techniques
文献类型：期刊论文
| 作者 | Liu CW ; Bo AL ; Cheng GJ ; Lin XQ ; Dong SJ |
| 刊名 | biochimica et biophysica acta-protein structure and molecular enzymology
 |
| 出版日期 | 1998 |
| 卷号 | 1385期号:1页码:53-60 |
| 关键词 | TRANSFORM INFRARED-SPECTROSCOPY PROTEIN SECONDARY STRUCTURE CIRCULAR-DICHROISM CONFORMATIONAL-CHANGES BETA-LACTOGLOBULIN SPECTRA DENATURATION POLYPEPTIDES PEPTIDES FTIR |
| ISSN号 | 0167-4838 |
| 通讯作者 | dong sj |
| 中文摘要 | circular dichroism (cd), fourier transform infrared (ftir), and fluorescence spectroscopy were used to explore the effect of dimethyl sulfoxide (dmso) on the structure and function of hemoglobin (hb). the native tertiary structure was disrupted completely when the concentration of dmso reached 50% (v/v), which was determined by loss of the characteristic soret cd spectrum. loss of the native tertiary structure could be mainly caused by breaking the hydrogen bonds, between the heme propionate groups and nearby surface amino acid residues, and by disorganizing the hydrophobic interior of this protein. upon exposure of hb to 52% dmso for ca. 12 h in a d2o medium no significant change in 1652 cm(-1) band of the ftir spectrum was produced, which demonstrated that alpha-helical structure predominated. when the concentration of dmso increased to 57%: (1) the band at 1652 cm(-1) disappeared with the appearance of two new bands located at 1661 and 1648 cm(-1); (2) another new band at 1623 cm(-1) was attributed to the formation of intermolecular beta-sheet or aggregation, which was the direct consequence of breaking of the polypeptide chain by the competition of s=o groups in dmso with c=o groups in amide bonds. further increasing the dmso concentration to 80%, the intensity at 1623 cm(-1) increased, and the bands at 1684, 1661 and 1648 cm(-1) shifted to 1688, 1664 and 1644 cm(-1), respectively. these changes showed that the native secondary structure of hb was last and led to further aggregation and increase of the content of 'free' amide c=o groups. in pure dmso solvent, the major band at 1664 cm(-1) indicated that almost all of both the intermolecular beta-sheet and any residual secondary structure were completely disrupted. the red shift of the fluorescence emission maxima showed that the tryptophan residues were exposed to a greater hydrophilic environment as the dmso content increased. go-binding experiment suggested that the biological function of hb was disrupted seriously even if the content of dmso was 20%. (c) 1998 elsevier science b.v. all rights reserved. |
| 收录类别 | SCI收录期刊论文 |
| 语种 | 英语 |
| WOS记录号 | WOS:000074465500006 |
| 公开日期 | 2010-11-04 |
| 源URL | [http://202.98.16.49/handle/322003/22887]  |
| 专题 | 长春应用化学研究所_长春应用化学研究所知识产出_期刊论文 |
| 推荐引用方式 GB/T 7714 | Liu CW,Bo AL,Cheng GJ,et al. Characterization of the structural and functional changes of hemoglobin in dimethyl sulfoxide by spectroscopic techniques[J]. biochimica et biophysica acta-protein structure and molecular enzymology,1998,1385(1):53-60. |
| APA | Liu CW,Bo AL,Cheng GJ,Lin XQ,&Dong SJ.(1998).Characterization of the structural and functional changes of hemoglobin in dimethyl sulfoxide by spectroscopic techniques.biochimica et biophysica acta-protein structure and molecular enzymology,1385(1),53-60. |
| MLA | Liu CW,et al."Characterization of the structural and functional changes of hemoglobin in dimethyl sulfoxide by spectroscopic techniques".biochimica et biophysica acta-protein structure and molecular enzymology 1385.1(1998):53-60. |
入库方式： OAI收割
来源：长春应用化学研究所
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