Protein Crystallization in Ionic-Liquid Hydrogel Composite Membranes
| Autor: | Rosanna Caliandro, Benny Danilo Belviso, Gianluca Di Profio, Rocco Caliandro, Shabnam Majidi Salehi |
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| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Glucose-6-phosphate isomerase
Materials science protein crystallization structural model comparison General Chemical Engineering Crystal growth 02 engineering and technology Crystal structure 010402 general chemistry 01 natural sciences law.invention Inorganic Chemistry ionic liquids chemistry.chemical_compound law lcsh:QD901-999 Molecule General Materials Science Crystallization 021001 nanoscience & nanotechnology Condensed Matter Physics 0104 chemical sciences Membrane chemistry Chemical engineering hydrogel composite membranes Ionic liquid glucose isomerase lcsh:Crystallography 0210 nano-technology Protein crystallization |
| Zdroj: | Crystals (Basel) 9 (2019). doi:10.3390/cryst9050253 info:cnr-pdr/source/autori:Belviso, Benny Danilo; Caliandro, Rosanna; Salehi, Shabnam Majidi; Di Profio, Gianluca; Caliandro, Rocco/titolo:Protein Crystallization in Ionic-Liquid Hydrogel Composite Membranes/doi:10.3390%2Fcryst9050253/rivista:Crystals (Basel)/anno:2019/pagina_da:/pagina_a:/intervallo_pagine:/volume:9 Crystals Volume 9 Issue 5 Crystals, Vol 9, Iss 5, p 253 (2019) |
| DOI: | 10.3390/cryst9050253 |
| Popis: | Protein crystallization is a powerful purification tool. It is the first step for crystallographic structural investigations, and can be preparatory for biotechnological applications. However, crystallizing proteins is challenging and methods to control the crystallization process are needed. Ionic-liquid hydrogel composite membranes (IL-HCMs) have been used here as material capable of supporting protein crystallization and hosting grown crystals. We found that IL-HCMs affect the selection mechanism of glucose isomerase (GI) polymorphs and make GI crystals grow completely immersed into the hydrogel layer. X-ray diffraction studies show that IL ions do not bind to the protein, likely because IL molecules are constrained in the polymeric framework. Our GI crystal structures have been compared with many existing GI crystal structures using multivariate analysis tools, allowing a comprehensive overview of factors determining structural similarities, i.e., temperature variations and external stresses exerted during or after crystal growth, such as dehydration or presence of hydrogel of a different nature. GI crystals grown on IL-HCM fit perfectly in this framework, showing typical features induced by external forces. Overall, protein crystallization by IL-HCMs show potential for biotechnological applications, as it could constitute a natural means for containing crystallized enzymes in working conditions. |
| Databáze: | OpenAIRE |
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