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Related Experiment Video

Updated: Jun 21, 2026

How to Measure Cortical Folding from MR Images: a Step-by-Step Tutorial to Compute Local Gyrification Index
09:57

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Slowing down downhill folding: a three-probe study.

Seung Joong Kim1, Yoshitaka Matsumura, Charles Dumont

  • 1Department of Physics, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.

Biophysical Journal
|July 8, 2009
PubMed
Summary
This summary is machine-generated.

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This study investigates the protein folding kinetics of a lambda repressor fragment mutant. By slowing down folding in cryogenic conditions, researchers found it folds faster than expected, suggesting a unique folding pathway.

Area of Science:

  • Protein folding dynamics
  • Biophysics
  • Molecular biology

Background:

  • Lambda repressor fragment lambda(6-85) mutant Tyr22Trp/Glu33Tyr/Gly46Ala/Gly48Ala is an incipient downhill folder.
  • Understanding protein folding pathways is crucial for molecular biology and disease research.

Purpose of the Study:

  • To investigate the refolding kinetics of a lambda repressor fragment mutant in cryogenic conditions.
  • To elucidate the folding mechanism and identify factors influencing folding speed.

Main Methods:

  • Cryogenic solvent (water-ethylene-glycol) at -18 to -28 degrees C.
  • Small-angle X-ray scattering (SAXS) to measure radius of gyration.
  • Circular dichroism (CD) for secondary structure content.
  • Fluorescence spectroscopy for native packing around tryptophan.

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Related Experiment Videos

Last Updated: Jun 21, 2026

How to Measure Cortical Folding from MR Images: a Step-by-Step Tutorial to Compute Local Gyrification Index
09:57

How to Measure Cortical Folding from MR Images: a Step-by-Step Tutorial to Compute Local Gyrification Index

Published on: January 2, 2012

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Revised and Neuroimaging-Compatible Versions of the Dual Task Screen
07:52

Revised and Neuroimaging-Compatible Versions of the Dual Task Screen

Published on: October 5, 2020

Main Results:

  • The mutant's main refolding phase is probe-independent and faster than the pseudo-wild-type.
  • Early formation of excess helical structure may prevent misfolded states.
  • Extrapolation to 37 degrees C indicates a refolding rate similar to previous NMR data.

Conclusions:

  • The mutant exhibits an accelerated folding process due to its unique structural properties.
  • The folding speed limit for this fast folder is approximately 4.5 microseconds.
  • Findings provide insights into the determinants of rapid protein folding.