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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...
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...
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...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...

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Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
22:00

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Published on: November 21, 2010

Membrane protein structure determination in membrana.

Yi Ding1, Yong Yao, Francesca M Marassi

  • 1Sanford-Burnham Medical Research Institute , 10901 North Torrey Pines Road, La Jolla, California 92037, United States.

Accounts of Chemical Research
|September 18, 2013
PubMed
Summary

Solid-state NMR spectroscopy determines membrane protein structures within lipid bilayers. This method uses orientation restraints to reveal 3D structures and protein orientation in natural membrane environments.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Biological membranes comprise lipid bilayers and proteins crucial for cell-environment interactions.
  • Understanding membrane protein structure is vital for elucidating cellular functions.
  • The interdependence of lipids and proteins necessitates structure determination within the native membrane environment.

Purpose of the Study:

  • To illustrate solid-state NMR methods for determining membrane protein structures in phospholipid bilayers.
  • To highlight the utility of orientation restraints for structural analysis of membrane proteins.
  • To showcase the application of these methods using bacterial outer membrane proteins OmpX and Ail.

Main Methods:

  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy, including oriented sample (OS) and magic angle spinning (MAS) approaches.
  • Utilizing (15)N/(13)C labeled samples for peak resolution and assignment.
  • Employing orientation restraints derived from spectral frequencies, combined with dihedral angle restraints, molecular fragment replacement, and de novo prediction.

Main Results:

  • Successful determination of three-dimensional structures for membrane proteins within lipid bilayers.
  • Demonstration that orientation restraints provide crucial information on both structure and protein orientation.
  • High-quality structures achieved with minimal reliance on distance restraints.

Conclusions:

  • Solid-state NMR is a powerful technique for 3D structure determination of membrane proteins in their native lipid environments.
  • Orientation restraints are key to understanding membrane protein structure and orientation.
  • Advancements in NMR technology and computational methods enable high-resolution structural studies of membrane proteins.