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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / chemistry
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Amino Acid Sequence
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Archaeal Proteins / metabolism
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Binding Sites
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Computer Simulation
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Disulfides
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Hot Temperature
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Hydrogen-Ion Concentration
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Models, Molecular
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Molecular Conformation
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Molecular Sequence Data
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NADH, NADPH Oxidoreductases / chemistry*
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Protein Conformation
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Protein Denaturation
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Protein Folding
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Protein Structure, Secondary
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Proteins / chemistry
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Pyrococcus furiosus / enzymology
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Pyrococcus furiosus / metabolism*
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Sodium Dodecyl Sulfate / chemistry*
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Spectrophotometry
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Spectroscopy, Fourier Transform Infrared
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Temperature
Substances
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Archaeal Proteins
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Disulfides
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Proteins
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Sodium Dodecyl Sulfate
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NADH, NADPH Oxidoreductases
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protein disulfide oxidoreductase, P. furiosus
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Adenosine Triphosphatases