The balance of flexibility and rigidity in the active site residues of hen egg white lysozyme
文献类型：期刊论文
| 作者 | Qi, JX ; Jiang, F |
| 刊名 | CHINESE PHYSICS B
 |
| 出版日期 | 2011 |
| 卷号 | 20期号:5 |
| 关键词 | INTRINSICALLY UNSTRUCTURED PROTEINS MOLECULAR INTERACTION DATABASE X-RAY-DIFFRACTION CONFORMATIONAL FLEXIBILITY SACCHAROMYCES-CEREVISIAE TEMPERATURE FACTORS REFINEMENT CRYSTALLOGRAPHY PARAMETERS YEAST |
| ISSN号 | 1674-1056 |
| 通讯作者 | Jiang, F (reprint author), Chinese Acad Sci, Beijing Natl Lab Condensed Matter Phys, Inst Phys, Beijing 100190, Peoples R China. |
| 中文摘要 | The crystallographic temperature factors (B factor) of individual atoms contain important information about the thermal motion of the atoms in a macromolecule. Previously the theory of flexibility of active site has been established based on the observation that the enzyme activity is sensitive to low concentration denaturing agents. It has been found that the loss of enzyme activity occurs well before the disruption of the three-dimensional structural scaffold of the enzyme. To test the theory of conformational flexibility of enzyme active site, crystal structures were perturbed by soaking in low concentration guanidine hydrochloride solutions. It was found that many lysozyme crystals tested could still diffract until the concentration of guanidine hydrochloride reached 3 M. It was also found that the B factors averaged over individually collected data sets were more accurate. Thus it suggested that accurate measurement of crystal temperature factors could be achieved for medium-high or even medium resolution crystals by averaging over multiple data sets. Furthermore, we found that the correctly predicted active sites included not only the more flexible residues, but also some more rigid residues. Both the flexible and the rigid residues in the active site played an important role in forming the active site residue network, covering the majority of the substrate binding residues. Therefore, this experimental prediction method may be useful for characterizing the binding site and the function of a protein, such as drug targeting. |
| 收录类别 | SCI |
| 资助信息 | National Natural Science Foundation of China [10674172, 10874229] |
| 语种 | 英语 |
| 公开日期 | 2013-09-23 |
| 源URL | [http://ir.iphy.ac.cn/handle/311004/44903]  |
| 专题 | 物理研究所_物理所公开发表论文_物理所公开发表论文_期刊论文 |
| 推荐引用方式 GB/T 7714 | Qi, JX,Jiang, F. The balance of flexibility and rigidity in the active site residues of hen egg white lysozyme[J]. CHINESE PHYSICS B,2011,20(5). |
| APA | Qi, JX,&Jiang, F.(2011).The balance of flexibility and rigidity in the active site residues of hen egg white lysozyme.CHINESE PHYSICS B,20(5). |
| MLA | Qi, JX,et al."The balance of flexibility and rigidity in the active site residues of hen egg white lysozyme".CHINESE PHYSICS B 20.5(2011). |
入库方式： OAI收割
来源：物理研究所
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