Cioni P. 1, Strambini G.B. 1
1: CNR
After a brief introduction of the potentialities of Trp phosphorescence spectroscopy for probing the conformation and flexibility of protein structure, this presentation summarizes the effects of hydrostatic pressure (up to 3 kbar) on the native fold of monomeric and oligomeric proteins as inferred from the variation of the intrinsic phosphorescence lifetime and the oxygen and acrylamide bimolecular quenching rate constants of buried Trp residues. The pressure/temperature response of the globular fold and modulation of its dynamical structure is analyzed both in terms of a reduction of internal cavities and of hydration of the polypeptide. The implications of these findings for the thermodynamic stability of proteins and for the determination of subunit dissociation equilibria under high pressure conditions are also discussed.
High pressure, Tryptophan, phosphorescence, Protein dynamics, Protein structure
Strambini Giovanni Battista, Cioni Patrizia
ID: 9327
Year: 2002
Type: Articolo in rivista
Creation: 2009-06-16 00:00:00.000
Last update: 2009-06-16 00:00:00.000
CNR authors
CNR institutes
External IDs
CNR OAI-PMH: oai:it.cnr:prodotti:9327