Cargando…
Water-Membrane Partition Thermodynamics of an Amphiphilic Lipopeptide: An Enthalpy-Driven Hydrophobic Effect
To shed light on the driving force for the hydrophobic effect that partitions amphiphilic lipoproteins between water and membrane, we carried out an atomically detailed thermodynamic analysis of a triply lipid modified H-ras heptapeptide anchor (ANCH) in water and in a DMPC (1,2-dimyristoyl-sn-glyce...
Autores principales: | Gorfe, Alemayehu A., Baron, Riccardo, McCammon, J. Andrew |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Biophysical Society
2008
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2547422/ https://www.ncbi.nlm.nih.gov/pubmed/18621822 http://dx.doi.org/10.1529/biophysj.108.136481 |
Ejemplares similares
-
How Can Hydrophobic Association Be Enthalpy Driven?
por: Setny, Piotr, et al.
Publicado: (2010) -
Hydrophobic Mismatch Drives the Interaction of E5 with the Transmembrane Segment of PDGF Receptor
por: Windisch, Dirk, et al.
Publicado: (2015) -
Thermodynamics of Peptide Insertion and Aggregation in a Lipid Bilayer
por: Babakhani, Arneh, et al.
Publicado: (2008) -
Similar Membrane Affinity of Mono- and Di-S-acylated Ras Membrane Anchors: A New Twist in the Role of Protein Lipidation
por: Gorfe, Alemayehu A., et al.
Publicado: (2008) -
Pilot-scale spiral wound membrane assessment for THM precursor rejection from upland waters
por: Golea, D., et al.
Publicado: (2016)