Abstract
The solid-phase chemical synthesis of ubiquitin produced a molecule with physicochemical properties similar to those of the natural protein. We have grown crystals of this synthetic ubiquitin and performed an X-ray analysis at 1.8 Å resolution in order to compare the synthetic protein with the known natural structure. The crystals were isomorphous with those of the natural protein, the R-factor between them being 7.1%. Difference Fourier analysis shows that the synthetic and natural structures are indistinguishable. The co-ordinates of the natural ubiquitin (IUBQ) were used as the starting point for restrained least-squares refinement (TNT program) against the synthetic X-ray data. The refinement converged to R = 16.5% and the resulting model did not change when refined against natural ubiquitin X-ray data (R = 18.7%). From both the refinement and featureless difference Fourier synthesis, we conclude that the synthetic and natural protein structures are identical. A short discussion about the uses of proteins with 'non-standard' amino acid residues is included.
Original language | English (US) |
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Pages (from-to) | 159-163 |
Number of pages | 5 |
Journal | Biochemical Journal |
Volume | 299 |
Issue number | 1 |
DOIs | |
State | Published - 1994 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Biochemistry
- Cell Biology