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Literature summary for 4.6.1.18 extracted from

  • Font, J.; Torrent, J.; Ribo, M.; Laurents, D.V.; Balny, C.; Vilanova, M.; Lange, R.
    Pressure-jump-induced kinetics reveals a hydration dependent folding/unfolding mechanism of ribonuclease A (2006), Biophys. J., 91, 2264-2274.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
Y115W fluorescent enzyme variant Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
study on folding/unfolding by pressure-jump-induced relaxation kinetics. Downward pressure jumps result always in single exponential kinetics, while upward jumps are biphasic in the low pressure range and monophasic at higher pressures. Analysis of the activation volume shows a temperature-dependent shift of the unfolding transition state to a larger volume Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
Bos taurus
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