Abstract
The ability to specifically incorporate artificial transition metal binding sites into proteins has led to the development of novel biomolecules with unique chemical and physical properties.1 Recent experiments demonstrate that such “engineered” sites of metal ion binding can, for example, assist in the conformational stabilization and assembly of polypeptides2 or serve to regulate enzymatic activity.3 In addition, the specific incorporation of redox-active metal ions, capable of generating oxidizing equivalents competent to cleave the polymeric backbone of proteins or nucleic acids, has facilitated investigations of protein three-dimensional structure,4 folding,5 and involvement in macromolecular binding interactions through affinity cleavage experiments (e.g., with nucleic acids).6 A growing appreciation of the utility of artificial metal binding domains has therefore accelerated the development of new methodologies which permit their efficient and specific installation within the tertiary structures of proteins.
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Long, E.C., Eason, P.D., Shullenberger, D.F. (1996). Incorporation of Square-Planar Metal Binding Sites into Protein Polymeric Structures. In: Pittman, C.U., Carraher, C.E., Zeldin, M., Sheats, J.E., Culbertson, B.M. (eds) Metal-Containing Polymeric Materials. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0365-7_36
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DOI: https://doi.org/10.1007/978-1-4613-0365-7_36
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