This title appears in the Scientific Report :
2000
Molecular dynamics simulations of hydrophobic and amphiphatic proteins interacting with a lipid bilayer membrane
Molecular dynamics simulations of hydrophobic and amphiphatic proteins interacting with a lipid bilayer membrane
Molecular dynamics simulations of polypeptides at high dilution near a fully hydrated bilayer membrane have been performed. In contrast to previous theoretical predictions, Monte Carlo simulations and conclusions from experiments a spontaneous insertion of amphiphatic or hydrophobic proteins into a...
| Personal Name(s): | Lin, J.-H. |
|---|---|
| Baumgärtner, A. | |
| Contributing Institute: |
Institut für Festkörperforschung; IFF Forum Modellierung; MOD |
| Published in: | Computational and Theoretical Polymer Science, 10 (2000) S. 97 |
| Imprint: |
Amsterdam [u.a.]
Elsevier
2000
|
| Physical Description: |
97 |
| Document Type: |
Journal Article |
| Research Program: |
Modellierung komplexer Systeme Polymere, Membranen und komplexe Flüssigkeiten |
| Series Title: |
Computational and Theoretical Polymer Science
10 |
| Subject (ZB): | |
| Publikationsportal JuSER |
|
Molecular dynamics simulations of polypeptides at high dilution near a fully hydrated bilayer membrane have been performed. In contrast to previous theoretical predictions, Monte Carlo simulations and conclusions from experiments a spontaneous insertion of amphiphatic or hydrophobic proteins into a membrane is not observed. Rather it is found that an amphiphatic chain has the tendency to remain in proximity to the membrane surface, whereas the location of a hydrophobic chain is more unbound. This is shown using two proteins, melittin and polyleucine. The conformation of the proteins and their orientation with respect to the membrane surface are discussed. (C) 2000 Elsevier Science Ltd. All rights reserved. |