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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

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.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

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.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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.
The...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

Folding scene investigation: membrane proteins.

Paula J Booth1, Paul Curnow

  • 1Department of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, UK. paula.booth@bristol.ac.uk

Current Opinion in Structural Biology
|January 23, 2009
PubMed
Summary

Membrane protein folding is now more understood, with new methods adapting classical techniques. Advances in understanding interactions and transition states promise future breakthroughs in membrane protein folding research.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Biophysics

Background:

  • Membrane protein folding mechanisms remain largely unknown due to experimental challenges.
  • Previous research focused on soluble proteins, leaving membrane proteins understudied.
  • Alpha-helical membrane proteins present unique folding complexities.

Purpose of the Study:

  • To investigate the stabilizing interactions in folded alpha-helical membrane proteins.
  • To characterize the folding transition state of membrane proteins.
  • To explore the adaptability of classical protein folding methods for membrane proteins.

Main Methods:

  • Adaptation of classical biophysical techniques for membrane protein studies.
  • Analysis of interactions stabilizing the folded state.
  • Characterization of folding intermediates and transition states.

Main Results:

  • New evidence elucidates interactions stabilizing alpha-helical membrane proteins.
  • Insights into the nature of the membrane protein folding transition state were gained.
  • Demonstrated successful adaptation of classical methods for membrane protein folding.

Conclusions:

  • Classical methods can be effectively applied to study membrane protein folding.
  • Recent advances provide a strong foundation for future research in this area.
  • Increased availability of crystal structures will accelerate understanding of membrane protein folding mechanisms.