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Related Concept Videos

Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
Molecular Chaperones and Protein Folding03:00

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Membrane Fluidity01:23

Membrane Fluidity

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.Fatty acids tails of phospholipids can be either saturated or...
Membrane Fluidity01:26

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Mosaic nature of the membrane
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Related Experiment Video

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A Fluorescence-based Assay of Phospholipid Scramblase Activity
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Published on: September 20, 2016

Opsin stability and folding: modulation by phospholipid bicelles.

Craig McKibbin1, Nicola A Farmer, Chris Jeans

  • 1Department of Biochemistry, University of Bristol, Bristol BS8 1TD, UK. craig.mckibbin@manchester.ac.uk

Journal of Molecular Biology
|November 13, 2007
PubMed
Summary

Phospholipid bicelles stabilize integral membrane proteins like rhodopsin and opsin in vitro. These bicelles, particularly those with Chaps, enhance protein stability and preserve secondary structure, aiding in structural and functional studies.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Protein Research

Background:

  • Integral membrane proteins are often unstable when extracted from biological membranes using common detergents.
  • Detergent-based methods can lead to loss of activity and structural integrity, hindering research.
  • Alpha-helical membrane proteins, such as rhodopsin, require specific environments for stability.

Purpose of the Study:

  • To investigate the efficacy of phospholipid bicelles in stabilizing alpha-helical membrane proteins in vitro.
  • To compare the stabilizing effects of different bicelle compositions (DMPC/Chaps and DMPC/DHPC) on rhodopsin and opsin.
  • To explore how bicelle properties, like the q value, influence protein stability and secondary structure preservation.

Main Methods:

  • Purification of opsin and rhodopsin into DMPC/Chaps and DMPC/DHPC bicelles.
  • Assessment of protein stability and secondary structure using synchrotron far-UV circular dichroism spectroscopy.
  • Regeneration of rhodopsin to determine functional recovery.
  • Modulation of bicelle properties (q value) to study their impact on protein stability.

Main Results:

  • Both DMPC/Chaps and DMPC/DHPC bicelles significantly increased the stability of rhodopsin and opsin.
  • Opsin was directly purified into DMPC/Chaps bicelles, and functional opsin was obtained in DMPC/DHPC bicelles with ~70% rhodopsin regeneration yield.
  • Opsin stability in DMPC/DHPC bicelles correlated with the q value, indicating modulation by bicelle size and composition.
  • DMPC/Chaps bicelles provided the greatest stability, suggesting Chaps contributes beyond the bilayer fragment itself.

Conclusions:

  • Phospholipid bicelles are effective tools for stabilizing alpha-helical membrane proteins, including rhodopsin and opsin, in a soluble and active state.
  • Bicelle composition, particularly the presence of Chaps, plays a crucial role in enhancing protein stability and preserving secondary structure.
  • These findings are relevant for studying other challenging membrane proteins, such as G-protein-coupled receptors, which are often unstable in detergents.