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 R-helices and â-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.
TEMPERATURE-, SDS-, AND PH-INDUCED CONFORMATIONAL CHANGES IN PROTEIN DISULFIDE / Pedone, E; Saviano, M; Bartolucci, Simonetta; Rossi, Mose'; Ausili, A; Scire, A; Beroli, E; Tanfani, F.. - In: JOURNAL OF PROTEOME RESEARCH. - ISSN 1535-3893. - STAMPA. - 4:6(2005), pp. 1972-1980. [10.1021/pr050152z]
TEMPERATURE-, SDS-, AND PH-INDUCED CONFORMATIONAL CHANGES IN PROTEIN DISULFIDE
BARTOLUCCI, SIMONETTA;ROSSI, MOSE';
2005
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 R-helices and â-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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
