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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

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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...
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 and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

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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

Membrane protein folding: how important are hydrogen bonds?

James U Bowie1

  • 1Department of Chemistry and Biochemistry, UCLA-DOE Institute of Genomics and Proteomics, Molecular Biology Institute, University of California, Los Angeles, USA. bowie@mbi.ucla.edu

Current Opinion in Structural Biology
|November 16, 2010
PubMed
Summary

Protein hydrogen bonds are weaker in membranes than expected. The protein environment, not just the apolar solvent, creates competing interactions that weaken these crucial bonds.

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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
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Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Biophysics

Background:

  • Water's polarity hinders protein hydrogen bonds.
  • Apolar membrane cores were assumed to favor strong hydrogen bonds for protein folding.
  • Previous assumptions about membrane protein stability lacked consideration of the protein's internal environment.

Purpose of the Study:

  • To investigate the actual strength of side chain hydrogen bonds in membrane proteins.
  • To understand why side chain hydrogen bond strengths in membrane proteins are similar to those in water-soluble proteins.
  • To challenge the assumption that apolar environments inherently maximize hydrogen bond strength in proteins.

Main Methods:

  • Comparative analysis of experimental data on hydrogen bond strengths.
  • Theoretical consideration of the protein's internal environment and its effect on hydrogen bonds.
  • Utilizing model compounds in apolar solvents for comparison.

Main Results:

  • Side chain hydrogen bond strengths in membrane proteins are not significantly stronger than in water-soluble proteins.
  • Backbone hydrogen bonds may be stronger in membrane proteins.
  • Apolar solvents alone do not fully explain hydrogen bond behavior in membrane proteins.

Conclusions:

  • The protein chain itself provides a polarizable environment and competitive hydrogen bonds that weaken interactions.
  • The assumption that apolar environments maximize hydrogen bond strength is an oversimplification.
  • Evolutionary forces must overcome these internal mitigating factors to create strong, functional hydrogen bonds in membrane proteins.