Literature summary for 4.6.1.18 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.

Search for more literature for 4.6.1.18

Protein Variants

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

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)