http://www.cnr.it/ontology/cnr/individuo/prodotto/ID50647
Investigation on Radical-Based Damage of RNase A in Aqueous Solutions and Lipid Vesicles (Articolo in rivista)
- Type
- Label
- Investigation on Radical-Based Damage of RNase A in Aqueous Solutions and Lipid Vesicles (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/bip.20375 (literal)
- Alternative label
Torreggiani, A.; Tamba, M.; Manco, I.; Faraone-Mennella, M. R.; Ferreri, C.; Chatgilialoglu, C. (2006)
Investigation on Radical-Based Damage of RNase A in Aqueous Solutions and Lipid Vesicles
in Biopolymers (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Torreggiani, A.; Tamba, M.; Manco, I.; Faraone-Mennella, M. R.; Ferreri, C.; Chatgilialoglu, C. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
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- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto I.S.O.F., Consiglio Nazionale delle Ricerche, Via P. Gobetti 101, 40129 Bologna, Italy
Dipartimento di Chimica Biologica, Università di Napoli, via Mezzocannone 16, 80134 Napoli, Italy (literal)
- Titolo
- Investigation on Radical-Based Damage of RNase A in Aqueous Solutions and Lipid Vesicles (literal)
- Abstract
- The ?-irradiation of bovine pancreatic ribonuclease A (RNase A) in aqueous solution were investigated at different doses by vibrational spectroscopy as well as enzymatic assay, electrophoresis, and HPLC analysis. Both functional and structural changes of the protein were caused by attack of H. atoms and .OH radicals. In particular, Raman spectroscopy was shown to be a useful tool in identifying conformational changes of the protein structure and amino acidic residues that are preferential sites of the radical attack (i.e., tyrosine and methionine). After partial structural changes by the initial radical attack, the internal sulfur-containing amino acid residues were rendered susceptible to transformation. By using the biomimetic model of dioleoyl phosphatidyl choline vesicle suspensions containing RNase A, the damage to methione residues could be connected to a parallel alteration of membrane unsaturated lipids. In fact, thiyl radical species formed from protein degradation can diffuse into the lipid bilayer and cause isomerization of the naturally occurring cis double bonds. As a consequence, trans unsaturated fatty acids are formed in vesicles and can be considered to be markers of this protein damage. (literal)
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- Autore CNR
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