http://www.cnr.it/ontology/cnr/individuo/prodotto/ID169113
Temperature-, SDS-, and pH-Induced Conformational Changes in Protein Disulfide Oxidoreductase from the Archaeon Pyrococcus furiosus: A Dynamic Simulation and Fourier Transform Infrared Spectroscopic Study (Articolo in rivista)
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- Temperature-, SDS-, and pH-Induced Conformational Changes in Protein Disulfide Oxidoreductase from the Archaeon Pyrococcus furiosus: A Dynamic Simulation and Fourier Transform Infrared Spectroscopic Study (Articolo in rivista) (literal)
- Anno
- 2005-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1021/pr050152z (literal)
- Alternative label
Pedone E., Saviano M., Bartolucci S., Rossi M., Ausili A., Scire A., Bertoli E., Tanfani F. (2005)
Temperature-, SDS-, and pH-Induced Conformational Changes in Protein Disulfide Oxidoreductase from the Archaeon Pyrococcus furiosus: A Dynamic Simulation and Fourier Transform Infrared Spectroscopic Study
in Journal of proteome research (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Pedone E., Saviano M., Bartolucci S., Rossi M., Ausili A., Scire A., Bertoli E., Tanfani F. (literal)
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- Articolo scientifico su rivista internazionale (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto di Biostrutture e Bioimmagini, CNR,
Dipartimento di Biologia Strutturale e Funzionale, Universita` degli Studi
di Napoli Federico II.
§ Istituto di Biochimica delle Proteine, C.N.R.
| Istituto di Biochimica, Universita` Politecnica delle Marche (literal)
- Titolo
- Temperature-, SDS-, and pH-Induced Conformational Changes in Protein Disulfide Oxidoreductase from the Archaeon Pyrococcus furiosus: A Dynamic Simulation and Fourier Transform Infrared Spectroscopic Study (literal)
- Abstract
- The effect of SDS, pD, and temperature on the structure and stability of the protein disulfide oxidoreductase from Pyrococcus furiosus (PfPDO) was investigated by molecular dynamic (MD) simulations and FT-IR spectroscopy. pD affects the thermostability of alpha-helices and beta-sheets differently, and 0.5% or higher SDS concentration influences the structure significantly. The experiments allowed us to detect a secondary structural reorganization at a definite temperature and pD which may correlate with a high ATPase activity of the protein. The MD simulations supported the infrared data and revealed the different behavior of the N and C terminal segments, as well as of the two active sites. (literal)
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