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Identification of specific lipid-binding sites in integral membrane proteins.


ABSTRACT: Protein-lipid interactions are increasingly recognized as central to the structure and function of membrane proteins. However, with the exception of simplified models, specific protein-lipid interactions are particularly difficult to highlight experimentally. Here, we used molecular dynamics simulations to identify a specific protein-lipid interaction in lactose permease, a prototypical model for transmembrane proteins. The interactions can be correlated with the functional dependence of the protein to specific lipid species. The technique is simple and widely applicable to other membrane proteins, and a variety of lipid matrices can be used.

SUBMITTER: Lensink MF 

PROVIDER: S-EPMC2856259 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature

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Identification of specific lipid-binding sites in integral membrane proteins.

Lensink Marc F MF   Govaerts Cédric C   Ruysschaert Jean-Marie JM  

The Journal of biological chemistry 20100205 14


Protein-lipid interactions are increasingly recognized as central to the structure and function of membrane proteins. However, with the exception of simplified models, specific protein-lipid interactions are particularly difficult to highlight experimentally. Here, we used molecular dynamics simulations to identify a specific protein-lipid interaction in lactose permease, a prototypical model for transmembrane proteins. The interactions can be correlated with the functional dependence of the pro  ...[more]

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