PUMA
Istituto di Biofisica     
Cioni P. High pressure effects on protein flexibility as monitored by tryptophan phosphorescence. Roland Winter and Jiri Jonas (eds.). (NATO advanced study institute on High pressure molecular science). Dordrecht [etc.]: Kluwer, published in cooperation with NATO scientific affairs division,, 1999.
 
 
Abstract
(English)
The sensitivity of Trp phosphorescence to monitor changes in conformation of native proteins has been used in order to monitor the effects of high hydrostatic pressure on various protein systems. According to  the triplet probe reveals that compression up to 3 kbar enhances the rigidity of interior sites but renders more fluid peripheral regions of the macromolecule in proximity to the solvent. Pressure studies on oligomeric proteins show that considerable alterations of the native structure may be induced by pressure both on the oligomer and on dissociated subunits. These results point out that the thermodynamic parameters governing the subunit dissociation equilibrium, as derived from pressure studies may not adequately describe oligomer dissociation at atmospheric pressure.
Subject High pressure
Tryptophan phosphorescence
Protein flexibility
Conformational drift


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