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Related Concept Videos

Membrane Fluidity01:26

Membrane Fluidity

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Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is...
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Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
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Updated: May 1, 2026

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Membrane protein structural validation by oriented sample solid-state NMR: diacylglycerol kinase.

Dylan T Murray1, Conggang Li2, F Philip Gao3

  • 1National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida; Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida.

Biophysical Journal
|April 18, 2014
PubMed
Summary
This summary is machine-generated.

Oriented sample solid-state NMR validates membrane protein structures by comparing experimental data with predicted spectra from structural models. This method confirms structures in lipid bilayers, overcoming limitations of detergent-based assays for membrane proteins.

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Area of Science:

  • Structural Biology
  • Biophysics
  • Membrane Protein Research

Background:

  • Functional assays traditionally validate water-soluble protein structures but face challenges for membrane proteins due to differing environments (detergent vs. lipid bilayers).
  • Membrane protein structures are sensitive to their environment, making validation difficult when structural analysis occurs in detergents and functional assays in lipid bilayers.

Purpose of the Study:

  • To develop and demonstrate a general technique for validating membrane protein structures using oriented sample solid-state NMR.
  • To compare experimental solid-state NMR data with predictions from existing diacylglycerol kinase structures.

Main Methods:

  • Utilized oriented sample solid-state NMR to collect spectral data from diacylglycerol kinase.
  • Compared observed NMR data with spectral predictions derived from solution NMR (detergent micelle) and crystal (monoolein cubic phase) structures.
  • Analyzed structural perturbations induced by different environments and mutations.

Main Results:

  • Solution NMR structure in detergent micelles showed significant perturbations compared to experimental data.
  • Crystal structures, particularly wild-type monomers without crystal contacts, exhibited minimal perturbations, with predicted and observed NMR data being nearly identical.
  • Thermostabilized constructs, especially the A41C mutant, showed increased perturbations due to altered lipid bilayer interactions and hydrogen bonding.

Conclusions:

  • Oriented sample solid-state NMR provides a robust method for validating membrane protein structures in a lipid bilayer environment.
  • This technique minimizes data requirements and offers a reliable approach to assess the accuracy of membrane protein structural models.
  • The study highlights the importance of the membrane mimetic environment in determining accurate membrane protein structures.