Racemic & quasi-racemic protein crystallography enabled by chemical protein synthesis.
| Autor: | Kent SB; University of Chicago, USA. |
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| Jazyk: | angličtina |
| Zdroj: | Current opinion in chemical biology [Curr Opin Chem Biol] 2018 Oct; Vol. 46, pp. 1-9. Date of Electronic Publication: 2018 Apr 05. |
| DOI: | 10.1016/j.cbpa.2018.03.012 |
| Abstrakt: | A racemic protein mixture can be used to form centrosymmetric crystals for structure determination by X-ray diffraction. Both the unnatural d-protein and the corresponding natural l-protein are made by total chemical synthesis based on native chemical ligation-chemoselective condensation of unprotected synthetic peptide segments. Racemic protein crystallography is important for structure determination of the many natural protein molecules that are refractory to crystallization. Racemic mixtures facilitate the crystallization of recalcitrant proteins, and give diffraction-quality crystals. Quasi-racemic crystallization, using a single d-protein molecule, can facilitate the determination of the structures of a series of l-protein analog molecules. (Copyright © 2018 Elsevier Ltd. All rights reserved.) |
| Databáze: | MEDLINE |
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