Kinetic equivalence of the heat and cold structural transitions of λ6-85

Wei Y. Yang, Martin Gruebele

Research output: Contribution to journalArticlepeer-review


Heat- and cold-denatured proteins are considered separate thermodynamic states because temperature tuning requires the protein to pass through two 'soft' first-order phase transitions. When both pressure and temperature changes are allowed, the heat- and cold-denatured states of proteins can be interconverted without going through the native state. This raises the question of whether these states are distinguished from one another by their folding kinetics. For the Tyr22-Trp/Ala37Gly/Ala49Gly mutant of the 80 residue five-helix bundle protein λ6-85, we show that viscosity-corrected folding rates do not distinguish the cold- and heat-denatured states. We attribute this to a folding mechanism dominated by hydrophobic collapse. Our 'temperature-symmetric' approach offers an alternative to viscosity tuning with solvent additives in such cases.

Original languageEnglish (US)
Pages (from-to)565-573
Number of pages9
JournalPhilosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences
Issue number1827
StatePublished - Feb 15 2005


  • Cold denaturation
  • Heat denaturation
  • Kinetics
  • Phase transition
  • Pressure denaturation
  • Temperature jump

ASJC Scopus subject areas

  • Mathematics(all)
  • Engineering(all)
  • Physics and Astronomy(all)

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