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| Content Provider | Springer Nature Link |
|---|---|
| Author | Levtsova, O. V. Davletov, I. D. Sokolova, O. S. Shaitan, K. V. |
| Copyright Year | 2011 |
| Abstract | The methods of computer simulation in all-atom and coarse-grained approximations have been used to study specific interactions of the isolated domain I-BAR of the actin-binding protein IRSp53 with model membranes containing neutral phospholipids and those including negatively charged PI(4,5)P$_{2}$ phospholipids. It has been shown that the I-BAR domain does not interact with neutral lipids but induces bending of the synthetic membrane rich in negatively charged phospholipids. Clustering of charged lipids on the surface of the membrane at the sites of its interaction with the protein has been observed. This indicates that the interaction of I-BAR with negatively charged lipids is of electrostatic and hydrophobic nature. |
| Starting Page | 220 |
| Ending Page | 224 |
| Page Count | 5 |
| File Format | |
| ISSN | 00063509 |
| Journal | Biophysics |
| Volume Number | 56 |
| Issue Number | 2 |
| e-ISSN | 15556654 |
| Language | English |
| Publisher | SP MAIK Nauka/Interperiodica |
| Publisher Date | 2011-07-01 |
| Publisher Place | Dordrecht |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | molecular dynamics conformational changes protein-lipid interactions Biophysics and Biological Physics |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biophysics |
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