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Protein Folding01:22

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Protein Folding01:22

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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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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
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Detection-dependent kinetics as a probe of folding landscape microstructure.

Wei Yuan Yang1, Martin Gruebele

  • 1Center for Biophysics and Computational Biology and Department of Chemistry, University of Illinois at Urbana-Champaign, Illinois 61801, USA. weiyang@fas.harvard.edu

Journal of the American Chemical Society
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Protein folding landscapes have many energy minima, from slow proline isomerization to fast submicrosecond microstructures. Wavelength-dependent kinetics reveal these hidden protein folding dynamics and energy landscape roughness.

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Last Updated: Jul 10, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
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Published on: April 28, 2011

Microfluidic Mixers for Studying Protein Folding
12:42

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Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions
09:15

Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions

Published on: November 21, 2017

Area of Science:

  • Biophysics
  • Protein dynamics
  • Chemical kinetics

Background:

  • Protein folding landscapes are complex, featuring a hierarchy of energy minima.
  • These minima arise from factors like proline isomerization and inherent frustration in amino acid sequences.
  • The associated timescales span from hours to submicroseconds, with smaller microstructures being challenging to detect.

Purpose of the Study:

  • To investigate the folding/unfolding kinetics of the engineered trpzip2 peptide.
  • To explore the presence and characteristics of small energy landscape microstructures.
  • To estimate the roughness of the protein free energy surface.

Main Methods:

  • Measured folding/unfolding kinetics of the trpzip2 peptide.
  • Utilized tryptophan fluorescence at different wavelengths to probe distinct environments.
  • Analyzed wavelength-dependent kinetics on submicrosecond timescales (0.1–2 µs).

Main Results:

  • Different fluorescence wavelengths yielded distinct folding/unfolding rates.
  • Wavelength-dependent kinetics revealed populated microstructures with varying solvent exposure and dynamics.
  • A range of observed rates allowed for an estimation of the free energy surface roughness.

Conclusions:

  • The study provides evidence for diverse microstructures within the protein folding landscape.
  • These findings highlight the complexity of protein energy surfaces, even at small scales.
  • The methods used offer a way to probe and quantify the roughness of these energy landscapes.