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Literature summary extracted from

  • Font, J.; Benito, A.; Lange, R.; Ribo, M.; Vilanova, M.
    The contribution of the residues from the main hydrophobic core of ribonuclease A to its pressure-folding transition state (2006), Protein Sci., 15, 1000-1009.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
4.6.1.18 I106A thermodynamic analysis of pressure-unfolding and kinetics for positive pressure-jumps Bos taurus
4.6.1.18 I107A thermodynamic analysis of pressure-unfolding and kinetics for positive pressure-jumps Bos taurus
4.6.1.18 I81A thermodynamic analysis of pressure-unfolding and kinetics for positive pressure-jumps Bos taurus
4.6.1.18 V108A thermodynamic analysis of pressure-unfolding and kinetics for positive pressure-jumps Bos taurus
4.6.1.18 V47A thermodynamic analysis of pressure-unfolding and kinetics for positive pressure-jumps Bos taurus
4.6.1.18 V54A thermodynamic analysis of pressure-unfolding and kinetics for positive pressure-jumps Bos taurus
4.6.1.18 V57A thermodynamic analysis of pressure-unfolding and kinetics for positive pressure-jumps Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.18 Bos taurus
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Renatured (Commentary)

EC Number Renatured (Comment) Organism
4.6.1.18 study on enzyme folding and refolding kinetics using pressure-jump techniques. The structure of the transition state is a relatively uniformly expanded form half-way between the folded and unfoded states. The pressure-folding transition state looks like a collapsed globule with some secondary structure and a weakenend hydrophobic core Bos taurus