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Engineered Metal-Binding Proteins: Purification to Protein Folding
Abstract
Proteins can make use of metal ions to bind substrates, \nto maintain structure, to effect catalysis, and for \nallosteric control and regulation. In order to hold a particular \nmetal ion with high affinity and specificity, proteins form multidentate \nbinding pockets designed to fulfill both the chemical and \ngeometric bonding requirements of that metal. Metal recognition \ncan be engineered into proteins for applications such as protein \npurification.
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Cited by
Engineering Novel Metalloproteins: Design of Metal-Binding Sites into Native Protein Scaffolds
Lu, Y., Berry, S. M., & Pfister, T. D. (2001) · Chemical Reviews · doi:10.1021/cr0000574 · Cited by 375
AFT1: a mediator of iron regulated transcriptional control in Saccharomyces cerevisiae.
Yamaguchi‐Iwai, Y., Dancis, A., & Klausner, R. D. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07106.x · Cited by 358
Metal3D: a general deep learning framework for accurate metal ion location prediction in proteins
Dürr, S. L., Levy, A., & Rothlisberger, U. (2023) · Nature Communications · doi:10.1038/s41467-023-37870-6 · Cited by 88
Investigating Native Metal Ion Binding Sites in Mammalian Histidine-Rich Glycoprotein
Ackermann, K., Khazaipoul, S., Wort, J. L., Sobczak, A. I. S., Mkami, H. E., Stewart, A. J., & Bode, B. E. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c00587 · Cited by 24
Metadata
- Authors
- Arnold, F. H., & Haymore, B. L.
- Venue
- Science
- Published
- 1991-06-28
- Volume
- 252
- Issue
- 5014
- Pages
- 1796-1797
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2082120576
- Cited by
- 228
- References
- 0
- FWCI
- 5.96
- Type
- journal article
- Language
- en
- Open access
- closed
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- Arnold, F. H., & Haymore, B. L. (1991). Engineered Metal-Binding Proteins: Purification to Protein Folding. Science. https://doi.org/10.1126/science.1648261
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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.