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Metal Ions in Biological Systems
Abstract
Volume 38: Probing of Proteins by Metal Ions and Their Low-Molecular-Weight Complexes focuses on the vibrant area of probing enzymes or proteins by metal ions and small complexes. It offers a summary of the basic characteristics of the amide bond, emphasizing its proton and metal ion interactions, including a quantitative analysis of its hydrolysis and formation. Topics include Peptide bonds, footprinting, protein degradation, protein complexes, and protein cross-linking.
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Citations
Cited by
Structure and Action Mechanism of Ligninolytic Enzymes
Wong, D. W. S. (2009) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-008-8279-z · Cited by 892
Reversible interconversion of carbon dioxide and formate by an electroactive enzyme
Reda, T., Plugge, C. M., Abram, N. J., & Hirst, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801290105 · Cited by 561
Microbial decolorization and degradation of synthetic dyes: a review
Khan, R., Bhawana, P., & Fulekar, M. H. (2013) · Reviews in Environmental Science and Bio/Technology · doi:10.1007/s11157-012-9287-6 · Cited by 448
Peloquin, J. M., Campbell, K. A., Randall, D. W., Evanchik, M. A., Pecoraro, V. L., Armstrong, W. H., & Britt, R. D. (2000) · Journal of the American Chemical Society · doi:10.1021/ja002104f · Cited by 377
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
Metadata
- Venue
- CRC Press eBooks
- Publisher
- CRC Press
- Published
- 2001-01-30
- OpenAlex
- W2885743120
- Cited by
- 275
- References
- 0
- Type
- reference entry
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.