http://www.cnr.it/ontology/cnr/individuo/prodotto/ID9183
Effect of heavy water on protein flexibility (Articolo in rivista)
- Type
- Label
- Effect of heavy water on protein flexibility (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., Strambini G.B. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Titolo
- Effect of heavy water on protein flexibility (literal)
- Abstract
- The effects of heavy water (D2O) on internal dynamics of proteins were
assessed by both the intrinsic phosphorescence lifetime of deeply buried
Trp residues, which reports on the local structure about the triplet
probe, and the bimolecular acrylamide phosphorescence quenching rate
constant that is a measure of the average acrylamide diffusion coefficient
through the macromolecule. The results obtained with several protein
systems (ribonuclease T1, superoxide dismutase, beta-lactoglobulin, liver
alcohol dehydrogenase, alkaline phosphatase, and apo- and Cd-azurin)
demonstrate that in most cases D2O does significantly increase the
rigidity the native structure. With the exception of alkaline phosphatase,
the kinetics of the structure tightening effect of deuteration and rapid
compared with the rate of H/D exchange of internal protons, which would
then assign the dampening of structural fluctuations in D2O to a solvent
effect, rather than to stronger intramolecular D bonding. Structure
tightening by heavy water is generally amplified at higher temperature,
supporting a mostly hydrophobic nature of the underlying interaction, and
under conditions that destabilize the globular fold. (literal)
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