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Protein Crystals as Novel Microporous Materials
Cross-linked protein crystals (CLPCs) constitute a novel type of molecular sieves with high porosity. In order to characterize the fully hydrated CLPC, the method of macromolecular porosimetry was applied. This technique allows one to estimate the apparent pore sizes and pore size distribution in so...
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Published in: | Journal of the American Chemical Society 1998-05, Vol.120 (18), p.4290-4294 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Cross-linked protein crystals (CLPCs) constitute a novel type of molecular sieves with high porosity. In order to characterize the fully hydrated CLPC, the method of macromolecular porosimetry was applied. This technique allows one to estimate the apparent pore sizes and pore size distribution in solid and soft hydrated porous sorbents directly from size exclusion chromatography. According to this method, CLPCs offer a wide range of pore size (15−100 Å), porosity (0.5−0.8), and pore surface area (800−2000 m2/g). These CLPC materials can be made chemically and mechanically stable, and are capable of separating molecules by size, chemical structure, and chirality. |
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ISSN: | 0002-7863 1520-5126 |
DOI: | 10.1021/ja973449+ |