English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Energetics of the Transmembrane Peptide Sorting by Hydrophobic Mismatch

MPS-Authors
/persons/resource/persons276433

Fábián,  Balázs       
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Supplementary Material (public)
There is no public supplementary material available
Citation

Fábián, B., & Javanainen, M. (2024). Energetics of the Transmembrane Peptide Sorting by Hydrophobic Mismatch. The Journal of Physical Chemistry Letters, 15(20), 5344-5349. doi:10.1021/acs.jpclett.4c00651.


Cite as: https://hdl.handle.net/21.11116/0000-000F-4EC9-8
Abstract
Hydrophobic mismatch between a lipid membrane and embedded transmembrane peptides or proteins plays a role in their lateral localization and function. Earlier studies have resolved numerous mechanisms through which the peptides and membrane proteins adapt to mismatch, yet the energetics of lateral sorting due to hydrophobic mismatch have remained elusive due to the lack of suitable computational or experimental protocols. Here, we pioneer a molecular dynamics simulation approach to study the sorting of peptides along a membrane thickness gradient. Peptides of different lengths tilt and diffuse along the membrane to eliminate mismatch with a rate directly proportional to the magnitude of mismatch. We extract the 2-dimensional free energy profiles as a function of local thickness and peptide orientation, revealing the relative contributions of sorting and tilting, and suggesting their thermally accessible regimes. Our approach can readily be applied to study other membrane systems of biological interest where hydrophobic mismatch, or membrane thickness in general, plays a role.