Articolo in rivista, 2002,

Tryptophan phosphorescence and pressure effects on protein structure

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.

Keywords

High pressure, Tryptophan, phosphorescence, Protein dynamics, Protein structure

CNR authors

Strambini Giovanni Battista, Cioni Patrizia

CNR institutes

IBF – Istituto di biofisica

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

External links

OAI-PMH: Dublin Core

OAI-PMH: Mods

OAI-PMH: RDF

External IDs

CNR OAI-PMH: oai:it.cnr:prodotti:9327