Posted in Organic Chemistry

Coordination Chemistry in Protein Cages: Principles, Design,

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

Featuring contributions from a workforce of foreign specialists within the coordination chemistry of organic structures, this e-book allows readers to appreciate and reap the benefits of the attention-grabbing inner molecular surroundings of protein cages. via smooth natural and polymer options, the authors clarify step-by-step tips on how to layout and build various protein cages. furthermore, the authors describe present purposes of protein cages, surroundings the root for the improvement of latest functions in biology, nanotechnology, artificial chemistry, and different disciplines.

Based on a radical evaluate of the literature in addition to the authors' personal laboratory adventure, Coordination Chemistry in Protein Cages

Sets forth the rules of coordination reactions in traditional protein cages
Details the basic 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 functions of protein cages in biology and nanotechnology
Describes the foundations of coordination chemistry that govern self-assembly of man-made cage-like molecules
Chapters are full of unique figures to assist readers comprehend the complicated constitution, layout, and alertness of protein cages. huge references on the finish of every bankruptcy function a gateway to special unique learn experiences and stories within the field.

With its particular overview of easy rules, 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 info for Coordination Chemistry in Protein Cages: Principles, Design, and Applications

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Theil, E. ; Bertini, I. Proc. Natl. Acad. Sci. USA 2010, 107, 545–550. ; Tsernoglou, D. Nat. Struct. Biol. 2000, 7, 38–43. ; Ceci, P. Biochim. Biophys. Acta 2010, 1800, 798–805. ; Allewell, N. ; Theil, E. C. J. Biol. Chem. 1998, 273, 18685–18688. Theil, E. ; Liu, X. ; Tosha, T. Inorganica Chim. Acta 2008, 361, 868–874. Banyard, S. ; Stammers, D. ; Harrison, P. M. Nature 1978, 271, 282–284. ; Chiancone, E. Biochemistry 1989, 28, 378–382. ; Chait, B. ; MacKinnon, R. Nature 2003, 423, 33–41. ; Ripoll, D.

Protons (2H+ /Fe) generated by hydrolysis of water, coordinated to ferric ions during catalysis/mineral nucleation/mineral growth, diffuse from the protein to the solution. Still unknown is how the diferric oxo reaction products are propelled into and along the nucleation channels (Fig. 5a). Possibly changes in acidity of water coordinated to iron during oxidation contribute to di-Fe(iii)O release. ) changes are occurring during diferric oxo product release and mineral nucleation. In some bacterial ferritin, such as the Dps proteins that protect DNA against the oxidative damage, the putative Fox site is on the inner surface of the protein cavity at the dimer interfaces, rather than in the center of each subunit, as seen in eukaryotic ferritin.

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. Sci. USA 2008, 105, 18182– 18187. ; Mayne, H. ; Chasteen, N. D. J. Am. Chem. Soc. 2005, 127, 3885–3893. ; Liu, X.

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