Mechanical unfolding of single bacteriorhodopsins from a membrane bilayer is studied using molecular dynamics simulations. The initial conformation of the lipid membrane is determined through all-atom simulations and then its coarse-grained representation is used in the studies of stretching. A Go-like model with a realistic contact map and with Lennard-Jones contact interactions is applied to model the protein-membrane system. The model qualitatively reproduces the experimentally observed differences between force-extension patterns obtained on bacteriorhodopsin at different temperatures and predicts a lack of symmetry in the choice of the terminus to pull by. It also illustrates the decisive role of the interactions of the protein with the membrane in determining the force pattern and thus the stability of transmembrane proteins.
|Number of pages||8|
|Journal||Biochimica et Biophysica Acta - Biomembranes|
|Publication status||Published - Apr 2006|
Bibliographical noteFunding Information:
This work was funded by the Ministry of Science and Informatics in Poland (grants 2P03B 03225 and 3P05F 02625). The modelling was partly done at the ICM Computer Centre, Warsaw University, Poland. HJ was supported by the European Union and the Free State of Saxony (grant to D. J. Mueller).
- Go model
- Mechanical stretching of protein
- Molecular dynamic