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
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(746 views) Pedone E, Saviano M, Bartolucci S, Rossi M, Ausili A, Scire A, Bertoli E, Tanfani F
J Proteome Res (ISSN: 1535-3893), 2005 Nov; 4(6): 1972-1980.
Keywords: Ft-Ir Spectroscopy, Md Simulations, Protein Disulfide Oxidoreductase, Protein Structure, Pyrococcus Furiosus, Thermostability, Adenosine Triphosphatase, Bacterial Enzyme, Protein Disulfide Reductase (glutathione), Archaebacterium, Article, Computer Simulation, Enzyme Active Site, Enzyme Activity, Fourier Transformation, Infrared Spectroscopy, Molecular Dynamics, Nonhuman, Priority Journal, Protein Conformation, Protein Secondary Structure, Temperature Dependence, Amino Acid Sequence, Archaeal Proteins, Binding Sites, Hydrogen-Ion Concentration, Models, Molecular Conformation, Molecular Sequence Data, Nadph Oxidoreductases, Protein Denaturation, Protein Folding, Sodium Dodecyl Sulfate, Spectrophotometry, Fourier Transform Infrared, Bacteria (microorganisms),
Affiliations: *** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, C.N.R, Via Mezzocannone 16, 80134, Napoli, Italy
Dipartimento di Biologia Strutturale e Funzionale, Università degli Studi di Napoli Federico II, via Mezzocannone 16, 80134 Napoli, Italy
Istituto di Biochimica Delle Proteine, C.N.R, via P. Castellino 111, 80131, Napoli, Italy
References: Not available.
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
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.
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
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