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Related Concept Videos

Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

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Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
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Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich...
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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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Membrane protein structure from rotational diffusion.

Bibhuti B Das1, Sang Ho Park1, Stanley J Opella1

  • 1Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA 92093-0307 USA.

Biochimica Et Biophysica Acta
|April 22, 2014
PubMed
Summary
This summary is machine-generated.

Rotationally aligned solid-state NMR (RA-NMR) determines membrane protein structures in phospholipid bilayers. This method uses motional averaging to provide accurate 3D structures under near-native conditions.

Keywords:
Membrane proteinNMR spectroscopyPhospholipid bilayerProtein structure determinationRotational diffusion

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Area of Science:

  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy
  • Structural biology
  • Membrane protein biophysics

Background:

  • Solid-state NMR is fundamental for studying molecular structures.
  • Membrane proteins in bilayers undergo rotational diffusion, influencing NMR signals.
  • Understanding membrane protein structure is crucial for biological function.

Purpose of the Study:

  • To present rotationally aligned (RA) solid-state NMR as a method for determining membrane protein structures.
  • To demonstrate the utility of RA-NMR for unmodified membrane proteins in phospholipid bilayers.
  • To highlight the advantages of studying proteins under near-native conditions.

Main Methods:

  • Utilizing motional averaging of powder pattern line shapes in solid-state NMR.
  • Analyzing signals reflecting tensor orientations relative to the bilayer normal.
  • Applying RA-NMR to full-length, unmodified membrane proteins with varying trans-membrane helices.

Main Results:

  • RA-NMR provides structural restraints from frequency span and sign of powder patterns.
  • Demonstrated successful structure determination for proteins with one, two, and seven trans-membrane helices.
  • Showcased RA-NMR's complementarity to oriented sample (OS) NMR and its ability to avoid structural distortions.

Conclusions:

  • RA-NMR enables accurate and precise 3D structure determination of membrane proteins.
  • The method is advantageous for studying unmodified proteins in phospholipid bilayers under physiological conditions.
  • RA-NMR offers a general approach for near-native membrane protein structure elucidation.