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| Reference : Synthesis, purification and initial structural characterization of octarellin, a de novo... |
| Scientific journals : Article | |||
| Life sciences : Biochemistry, biophysics & molecular biology | |||
| http://hdl.handle.net/2268/20095 | |||
| Synthesis, purification and initial structural characterization of octarellin, a de novo polypeptide modelled on the alpha/beta-barrel proteins | |
| English | |
| Goraj, Karine [> > > >] | |
| Renard, André [ > > ] | |
Martial, Joseph  [Université de Liège - ULg > Département des sciences de la vie > GIGA-R : Biologie et génétique moléculaire >] | |
| 1990 | |
| Protein Engineering | |
| Oxford University Press | |
| 3 | |
| 4 | |
| 259-66 | |
| 0269-2139 | |
| 1460-213X | |
| Oxford | |
| United Kingdom | |
| [en] Amino Acid Sequence ; Automatic Data Processing ; Base Sequence ; Circular Dichroism ; Cloning, Molecular ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli ; Molecular Sequence Data ; *Peptides/genetics ; Plasmids ; Protein Conformation ; *Protein Engineering | |
| [en] We have attempted to construct an artificial polypeptide that folds like the eight-stranded parallel beta-barrel structures. Our approach consists of repeating eight times a unit peptide designed to adopt a 'beta-strand/alpha-helix' pattern. A first 'test' sequence for this structural unit was deduced from a series of parameters defined after an analysis of three natural alpha/beta-barrel proteins and including principally the lengths of the secondary structure elements, the alpha/beta packing and the fitting on average Garnier profiles. The gene encoding this structural unit was synthesized, cloned and expressed in Escherichia coli either as a monomer or as direct repeats of 2-12 units. Preliminary structural characterization of the 7-, 8- and 9-fold unit polypeptides by circular dichroism measurements indicates the presence of the predicted amount of alpha-helix in the three proteins. Further analysis by urea-gradient gel electrophoresis demonstrates that, in the conditions tested, only the 8-fold unit polypeptide forms a compact structure through a cooperative and rapid two-state folding transition involving long-range molecular interactions. | |
| http://hdl.handle.net/2268/20095 | |
| http://peds.oxfordjournals.org/cgi/content/abstract/3/4/259 | |
| 1990/03/01 |
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