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Related Concept Videos

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 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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Bacterial Protein Maturation01:26

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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...

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Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
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Published on: December 12, 2017

Solvent-induced protein refolding at low temperatures.

Yasar Akdogan1, Dariush Hinderberger

  • 1Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany.

The Journal of Physical Chemistry. B
|November 26, 2011
PubMed
Summary

Low temperatures promote protein refolding in complex mixtures. Human serum albumin (HSA) unfolds with ethanol or ionic liquids but refolds upon cooling, as shown by electron paramagnetic resonance (EPR) spectroscopy.

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Area of Science:

  • Biophysics
  • Protein Chemistry
  • Spectroscopy

Background:

  • Human serum albumin (HSA) interactions with fatty acids (FAs) are crucial for biological functions.
  • Understanding protein folding and unfolding mechanisms is essential in biochemistry.
  • Electron paramagnetic resonance (EPR) spectroscopy is a powerful tool for studying protein dynamics.

Purpose of the Study:

  • To investigate the refolding of human serum albumin (HSA) at low temperatures in the presence of denaturing cosolvents.
  • To characterize the binding of spin-labeled fatty acids (FAs) to HSA during refolding using EPR techniques.
  • To explore the influence of ternary solvent mixtures on protein stability and solvation.

Main Methods:

  • Utilized continuous wave electron paramagnetic resonance (CW EPR) and double electron-electron resonance (DEER) spectroscopy.
  • Employed ternary solvent mixtures containing human serum albumin (HSA), spin-labeled fatty acids (FAs), and cosolvents (ethanol or ionic liquids).
  • Varied temperature conditions to induce and observe protein unfolding and refolding.

Main Results:

  • At room temperature, ethanol or ionic liquids denatured HSA, altering FA binding site signatures.
  • Decreasing temperature induced partial refolding of HSA, evidenced by bimodal CW EPR spectra showing both bound and free FA signals.
  • DEER data corroborated the refolding of HSA at lower temperatures.

Conclusions:

  • Low temperatures enhance protein stability, enabling refolding of human serum albumin (HSA) even in the presence of denaturing agents.
  • Changes in preferential solvation, particularly by glycerol, contribute to the observed protein stabilization.
  • EPR spectroscopy effectively monitors protein conformational changes and FA interactions during refolding processes.