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Related Concept Videos

Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
Membrane Proteins01:30

Membrane Proteins

Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
Membrane Proteins01:30

Membrane Proteins

Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

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
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell types have...
Fluid Mosaic Model01:19

Fluid Mosaic Model

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 with the analogy of...

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Related Experiment Video

Updated: May 8, 2026

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)
08:14

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)

Published on: April 20, 2015

Membrane protein structure determination: back to the membrane.

Yong Yao1, Yi Ding, Ye Tian

  • 1Sanford Burnham Medical Research Institute, La Jolla, CA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|August 27, 2013
PubMed
Summary
This summary is machine-generated.

Solid-state NMR spectroscopy determines membrane protein structures within their native lipid environments. This method is crucial for understanding bacterial virulence proteins like OmpX and Ail.

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Last Updated: May 8, 2026

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Membrane proteins are vital for cellular functions but challenging to study structurally.
  • Understanding their structure in a native-like environment is key to elucidating their mechanisms.

Purpose of the Study:

  • To outline methods for structural determination of membrane proteins using solid-state NMR spectroscopy.
  • To demonstrate the application of these methods using bacterial virulence proteins.

Main Methods:

  • Incorporation of membrane proteins into proteoliposomes or planar lipid bilayers.
  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy techniques.
  • Protein expression, purification, and sample preparation protocols.

Main Results:

  • Demonstrated successful structure determination of OmpX and Ail using solid-state NMR.
  • Provided detailed protocols applicable to other membrane proteins.

Conclusions:

  • Solid-state NMR is a powerful technique for elucidating membrane protein structures in native-like environments.
  • This approach facilitates the study of proteins involved in bacterial virulence.