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Open AccessJournal ArticleDOI

Interaction of membrane proteins and lipids with solubilizing detergents.

TLDR
The nature of detergent binding by the membrane from a noncooperative to a cooperative interaction already below the critical micellar concentration is considered and it is concluded that in general binding as a monolayer ring, rather than as a micelle, is the most probable mechanism.
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This article is published in Biochimica et Biophysica Acta.The article was published on 2000-11-23 and is currently open access. It has received 985 citations till now. The article focuses on the topics: Integral membrane protein & Peripheral membrane protein.

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Citations
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The Structure of the Potassium Channel: Molecular Basis of K+ Conduction and Selectivity

TL;DR: The architecture of the pore establishes the physical principles underlying selective K+ conduction, which promotes ion conduction by exploiting electrostatic repulsive forces to overcome attractive forces between K+ ions and the selectivity filter.
Journal ArticleDOI

The interaction between bacteria and bile

TL;DR: The antimicrobial actions of bile are described, the variations in bile tolerance between bacterial genera are assessed and the relationship between bile and virulence is examined.
Journal ArticleDOI

Lipid Rafts: Elusive or Illusive?

TL;DR: There has been considerable recent interest in the possibility that the plasma membrane contains lipid "rafts," microdomains enriched in cholesterol and sphingolipids, and it seems that a definitive proof of raft existence has yet to be obtained.
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Membrane proteins, lipids and detergents: not just a soap opera

TL;DR: This review will concentrate on the methods currently available for efficient reconstitution and solubilization of membrane proteins through the use of detergent micelles, mixed lipid/detergent micella and bicelles or liposomes and the role that lipids can play in stabilizing the proteins.
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Modern analytical ultracentrifugation in protein science: A tutorial review

TL;DR: Sedimentation equilibrium of proteins, including membrane proteins and glycoproteins, is the method of choice for molar mass determinations and the study of self‐association and heterogeneous interactions, such as protein–protein, protein–nucleic acid, and protein–small molecule binding.
References
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Journal ArticleDOI

Functional rafts in cell membranes

Kai Simons, +1 more
- 05 Jun 1997 - 
TL;DR: A new aspect of cell membrane structure is presented, based on the dynamic clustering of sphingolipids and cholesterol to form rafts that move within the fluid bilayer that function as platforms for the attachment of proteins when membranes are moved around inside the cell and during signal transduction.
Book

Surfactants and Interfacial Phenomena

TL;DR: In this paper, the Gibbs equation is used to calculate the area per Molecule at the interface by using the Gibbs Equation (GEE) of the Gibbs equilibrium. But the Gibbs equations are not applicable to surface-active agents.
Book

The Hydrophobic Effect: Formation of Micelles and Biological Membranes

TL;DR: In this article, the authors discuss the properties of water molecules and their relationship with common soluble proteins, such as membrane proteins and membrane membrane proteins, as well as the effect of temperature on their properties.
Journal ArticleDOI

Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution

TL;DR: The molecular structure of the photosynthetic reaction centre from Rhodopseudomonas viridis has been elucidated using X-ray crystallographic analysis and the first description of the high-resolution structure of an integral membrane protein is presented.
Journal ArticleDOI

Solubilization of membranes by detergents

TL;DR: This review focuses on work that deals with the mechanisms of detergent action in membrane solubilization including properties of detergents model lipid systems and detergent-protein interactions; in addition a possible sequence of events when deterGents interact with biological membranes receives attention.
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