Calbindin D9k Mutant: P20G + N21 deleted
Engineered mutant of calbindin D9k, from Bos taurus (InfoCard)
Similar Mutants:
General Effects of the Mutation:
- Apo state is slightly less stable to urea denaturation than apo wildtype protein is. Urea denaturation curve is almost identical to the curve for P20G alone (InfoCard)
- Macroscopic binding constants are lower than for wildtype calbindin, particularly K2. Interestingly, K1 is slightly higher than K1 for P20G alone, while K2 is about the same (within error bars) (InfoCard)
Physical Properties of the Mutant:
Stability:
Free energy of unfolding = 4.19 +/- 0.24 kcal/mol
cooperativity of unfolding = 0.836 kcal/(mol M)
(measured by: urea denaturation pH: 7.1 temperature: 25 degrees Celsius )
(InfoCard)
Ca Binding Constants (low salt:) :
K1 = 1.7 x 108 +/- 2 x 107; K2 = 5 x 108 +/- 2 x 108
(measured by: competitive chelator pH: 7.5 temperature: 25 degrees Celsius buffer: 0.002 M Tris-HCl )
(InfoCard)