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Experimental Methods for Investigation of Shape Memory Based Elastocaloric Cooling Processes and Model Validation
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Tuning lambda6-85 towards downhill folding at its melting temperature.

Feng Liu1, Martin Gruebele

  • 1Center for Biophysics and Computational Biology, University of Illinois, Urbana, IL 61801, USA. fengliu2@uiuc.edu

Journal of Molecular Biology
|May 29, 2007
PubMed
Summary

Investigating histidine-containing mutants of the lambda6-85* protein revealed that a weakened hydrophobic core can promote downhill protein folding over a wider temperature range. This finding advances understanding of protein folding energy landscapes.

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Area of Science:

  • Protein folding dynamics
  • Biophysics
  • Molecular biology

Background:

  • The lambda6-85* protein is a fast two-state folder, with some mutants exhibiting downhill folding kinetics.
  • A temperature-induced transition to two-state folding in these mutants is hypothesized to result from increased hydrophobicity at higher temperatures.

Purpose of the Study:

  • To investigate if a weaker hydrophobic core in histidine-containing lambda6-85* mutants can extend the temperature range of downhill folding.
  • To explore the folding kinetics and thermodynamic properties of specific lambda6-85* mutants (lambdaHA and lambdaHG).

Main Methods:

  • Characterization of two histidine-containing lambda6-85* mutants (lambdaHA and lambdaHG) with varying hydrophobic core strengths.
  • Kinetic analysis of protein folding and unfolding transitions using techniques like fluorescence spectroscopy.
  • Comparison of thermodynamic melting transitions between mutants with different folding behaviors.

Main Results:

  • The lambdaHA mutant, while very stable and fast-folding, transitions from downhill to two-state folding with increasing temperature.
  • The lambdaHG mutant, featuring a weakened hydrophobic core, exhibits incipient downhill folding kinetics even at its unfolding midpoint.
  • Thermodynamic analysis of lambdaHG revealed non-standard behavior, including fluorescence wavelength-dependent cooperativities and probe-dependent melting temperatures, unlike the two-state folding mutant lambdaQG.

Conclusions:

  • A weakened hydrophobic core can indeed promote downhill folding over an extended temperature range in lambda repressor mutants.
  • The energy landscapes of lambda repressor mutants are complex and can support diverse folding mechanisms, including those deviating from simple two-state models.