Physical characterization of a totally synthetic rubredoxin
| Autor: | Zhi H. Zhou, Michael W. W. Adams, Roberto P. Christen, Eugene T. Smith, John M. Tomich, Tatyana Jancic |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
chemistry.chemical_classification
Synthetic protein Hot Temperature biology Chemistry Rubredoxins Spectrum Analysis Molecular Sequence Data Peptide biology.organism_classification Biochemistry Archaea Characterization (materials science) Inorganic Chemistry Crystallography Paramagnetism Bacterial Proteins Rubredoxin Pyrococcus furiosus Electrochemistry Denaturation (biochemistry) Amino Acid Sequence Thermostability |
| Zdroj: | Journal of inorganic biochemistry. 65(1) |
| ISSN: | 0162-0134 |
| Popis: | The entire polypeptide of hyperthermophilic Pyrococcus furiosus rubredoxin was synthesized in order to specifically probe structural determinants of protein thermostability. The uv-visible, circular dichroic, electron paramagnetic, and nuclear magnetic resonance spectra, and electrochemical properties, of the native and synthetic proteins were essentially identical. The synthetic protein had a half-life for denaturation of 24 hr at 80°C. The synthetic protein is considerably more thermostable than nonhyperthermophilic rubredoxins, but not as stable as the native protein. Based on the spectroscopic evidence, it appears that the synthetic protein is incorporating iron properly to form holoprotein, but the peptide still may not be folded correctly. |
| Databáze: | OpenAIRE |
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