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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

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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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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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Microfluidic Mixers for Studying Protein Folding
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Published on: April 10, 2012

Exploring one-state downhill protein folding in single molecules.

Jianwei Liu1, Luis A Campos, Michele Cerminara

  • 1Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA.

Proceedings of the National Academy of Sciences of the United States of America
|December 21, 2011
PubMed
Summary

One-state downhill protein folding, a barrierless process, can be slowed for single-molecule observation. This study demonstrates one-state downhill folding kinetics at the single-molecule level using BBL protein.

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Area of Science:

  • Biophysics
  • Protein Folding Dynamics
  • Single-Molecule Biophysics

Background:

  • One-state downhill protein folding is a barrierless process, enabling step-by-step resolution of folding mechanisms.
  • Experimental studies often focus on ultrafast folding proteins, posing challenges for current single-molecule techniques like single-molecule Förster Resonance Energy Transfer (smFRET).
  • A key question is whether downhill folding kinetics can be slowed for single-molecule analysis without altering the folding mechanism.

Purpose of the Study:

  • To investigate if one-state downhill folding kinetics can be slowed to become accessible to single-molecule methods.
  • To demonstrate one-state downhill folding at the single-molecule level.
  • To explore the folding mechanism of the small helical protein BBL under slowed kinetics.

Main Methods:

  • Combined chemical denaturation and low temperature to decrease the folding-unfolding rate of BBL protein by 200-fold.
  • Conducted free-diffusion single-molecule Förster Resonance Energy Transfer (smFRET) experiments with 50-μs resolution.
  • Utilized a Trolox-cysteamine cocktail for maximal photoprotection during smFRET measurements.

Main Results:

  • Observed a single conformational ensemble across all denaturing conditions, indicating a unified folding pathway.
  • Demonstrated that chemical unfolding of BBL involves a gradual shift of this ensemble from high to low FRET efficiency as denaturant concentration increases.
  • Quantitative analysis ruled out overlapping folded and unfolded peaks, confirming the single-state nature of the observed data.

Conclusions:

  • Successfully demonstrated the one-state downhill folding regime at the single-molecule level.
  • Showed that one-state downhill folding is not exclusively associated with ultrafast kinetics.
  • Established that slowed downhill folding kinetics are achievable and observable with advanced single-molecule techniques.