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Units the level for the layout and alertness of recent protein cages

Featuring contributions from a crew of foreign specialists within the coordination chemistry of organic structures, this booklet allows readers to appreciate and make the most of the interesting inner molecular atmosphere of protein cages. through glossy natural and polymer options, the authors clarify step-by-step find out how to layout and build various protein cages. furthermore, the authors describe present functions of protein cages, environment the root for the advance of recent functions in biology, nanotechnology, artificial chemistry, and different disciplines.

Based on an intensive evaluation of the literature in addition to the authors' personal laboratory adventure, Coordination Chemistry in Protein Cages

Sets forth the rules of coordination reactions in average protein cages
Details the elemental layout of coordination websites of small synthetic metalloproteins because the foundation for protein cage design
Describes the supramolecular layout and meeting of protein cages for or through steel coordination
Examines the most recent purposes of protein cages in biology and nanotechnology
Describes the rules of coordination chemistry that govern self-assembly of artificial cage-like molecules
Chapters are jam-packed with particular figures to assist readers comprehend the complicated constitution, layout, and alertness of protein cages. broad references on the finish of every bankruptcy function a gateway to big unique examine reviews and reports within the field.

With its special overview of simple ideas, layout, and purposes, Coordination Chemistry in Protein Cages is usually recommended for investigators operating in organic inorganic chemistry, organic natural chemistry, and nanoscience.

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Additional resources for Coordination Chemistry in Protein Cages: Principles, Design, and Applications

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Theil, E. C. Proc. Natl. Acad. Sci. USA 2003, 100, 3653–3658. Theil, E. ; Goss, D. J. Chem. Rev. 2009, 109, 4568–4579. Bevers, L. ; Theil, E. C. Maxi- and mini-ferritins: minerals and protein nanocages. In Progress in Molecular and Subcellular Biology; Muller, W. E. ; Springer-Verlag: Berlin-Heidelberg, 2011; pp 18. ; Theil, E. C. Acc. Chem. Res. 2005, 38, 167–175. Crichton, R. ; Declercq, J. P. Biochim. Biophys. Acta 2010, 1800, 706–718. ; Ng, H. ; Theil, E. C. J. Am. Chem. Soc. 2010, 132, 14562–14569.

Seaman, W. E. Proc. Natl. Acad. Sci. USA 2011, 107, 3505–3510. ; Edmondson, D. ; Theil, E. ; Huynh, B. ; Loehr, T. M. Biochemistry 1999, 38, 5290–5295. ; Huynh, B. ; Edmondson, D. ; Theil, E. ; Penner-Hahn, J. E. Science 2000, 287, 122–125. ; Eklund, H. Curr. Opin. Chem. Biol. 1995, 5, 758–766. [42] Schwartz, J. ; Liu, X. ; Theil, E. ; Solomon, E. I. J. Am. Chem. Soc. 2008, 130, 9441–9450. ; Theil, E. C. Proc. Natl. Acad. Sci. USA 2004, 101, 8557–8562. ; Hasan, M. ; Theil, E. C. Proc. Natl. Acad.

As many as eight Fe(iii) ions are required to reach the end of the cavity, suggesting that iron mineral nuclei of significant size emerge into the cavity of the protein cage (Figs. 5). Each nucleation channel exit is near the exits of three other subunits around the fourfold symmetry axes of the protein cage (Figs. 4), which facilitate the ordered interactions of mineral nuclei from four subunits and the buildup of highly ordered ferritin minerals. If mineral nuclei from each active site are directed through intra-cage nucleation channels to exits from four subunits that are symmetrically clustered to form ordered minerals, how then do animals form less ordered ferritin mineral observed [54] in some tissue?

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