| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8290906 | Archives of Biochemistry and Biophysics | 2013 | 11 Pages |
Abstract
⺠[E43S]SNase retains the DNA-binding ability but loses its catalytic activity. ⺠Binding of ssDNA/Cd2+ to [E43S]SNase induced dynamics changes. ⺠Solution structure of ssDNA/Cd2+-bound [E43S]SNase was determined. ⺠[E43S]SNase-ssDNA-Cd2+ complex model was constructed based on experimental data. ⺠The model provide structural insight of the action of nuclease on ssDNA.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
![Modeling of the [E43S]SNase-ssDNA-Cd2+ complex: Structural insight into the action of nuclease on ssDNA](/preview/png/8290906.png "First Page Preview: Modeling of the [E43S]SNase-ssDNA-Cd2+ complex: Structural insight into the action of nuclease on ssDNA")
Authors
Tao Xie, Yingang Feng, Lu Shan, Jinfeng Wang,