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Related Concept Videos

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.
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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...
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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...
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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 proteins in four acts: function precedes structure determination.

W A Cramer1, S D Zakharov, S Saif Hasan

  • 1Department of Biological Sciences, Purdue University, Hall of Structural Biology, 240 Hockmeyer Hall, West Lafayette, IN 47907-1354, USA. waclab@purdue.edu

Methods (San Diego, Calif.)
|November 15, 2011
PubMed
Summary
This summary is machine-generated.

Functional assays are crucial for membrane protein crystallization. Biophysical and microbiological methods enable the study of diverse membrane protein systems, including electron transport complexes and outer membrane proteins.

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Area of Science:

  • Structural biology and biophysics of membrane proteins.

Background:

  • Crystallization of membrane proteins requires demonstration of functional activity.
  • Functional assays guide purification strategies for obtaining stable, crystallizable protein complexes.
  • Diverse membrane protein systems, including hetero-oligomeric complexes, beta-barrel outer membrane proteins, and intrinsically disordered proteins, were investigated.

Purpose of the Study:

  • To highlight the importance of functional assays in membrane protein crystallization.
  • To present studies combining structural and biophysical data for four distinct membrane protein systems.
  • To showcase advancements in purification and structural determination of challenging membrane proteins.

Main Methods:

  • Spectrophotometric assays for electron transfer.
  • Electrophysiological and channel analysis.
  • Microbiological screens for binding affinities.
  • Hydrophobic chromatography for lipid manipulation.
  • X-ray crystallography and lipid cubic phase methods.

Main Results:

  • Crystal structures of the cytochrome b(6)f complex and outer membrane proteins (BtuB, OmpF) were obtained.
  • Functional characterization of BtuB revealed its role in colicin import via a 'fishing pole' model.
  • OmpF structure elucidated its function as an import channel for colicin toxins.
  • Alpha-synuclein was shown to form voltage-gated ion channels upon membrane binding.

Conclusions:

  • Functional assays are indispensable for successful membrane protein structure determination.
  • Integrated structural and biophysical approaches provide deep insights into membrane protein mechanisms.
  • This work advances the understanding of electron transport, nutrient uptake, and disease-associated protein functions.