Article
Pressure effects on protein flexibility monomeric proteins.
Journal of molecular biology - 23 Sept 1994
Cioni P, Strambini G B
Abstract excerpt
Alterations in flexibility of monomeric proteins induced by hydrostatic pressure in the predenaturational range (< or = 3 kbar) were probed through the decay kinetics of tryptophan phosphorescence. With apoazurin, ribonuclease T1, wild-type and V67G mutant and phosphoglycerate kinase, pressure ef...
Topics
- Apoproteins
- Azurin
- Glycerol
- Hydrostatic Pressure
- Luminescent Measurements
- Mutation
- Phosphoglycerate Kinase
- Protein Conformation
- Protein Folding
- Ribonuclease T1
- Thermodynamics
- Tryptophan