http://www.cnr.it/ontology/cnr/individuo/prodotto/ID9327
Tryptophan phosphorescence and pressure effects on protein structure (Articolo in rivista)
- Type
- Label
- Tryptophan phosphorescence and pressure effects on protein structure (Articolo in rivista) (literal)
- Anno
- 2002-01-01T00:00:00+01:00 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Cioni P. 1, Strambini G.B. 1 (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Titolo
- Tryptophan phosphorescence and pressure effects on protein structure (literal)
- Abstract
- 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. (literal)
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- Autore CNR
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