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Biological Self-Assembly: A Paradigm for Materials Science

Published online by Cambridge University Press:  15 February 2011

Kevin P. McGrath  and
David L. Kaplan
Kevin P. McGrath
Affiliation:
Biotechnology Division, U.S. Army Natick RD&E Center Natick, MA 01760
David L. Kaplan
Affiliation:
Biotechnology Division, U.S. Army Natick RD&E Center Natick, MA 01760
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Abstract

Complex organized systems evolved from the prebiotic soup approximately three billion years ago, relying on simple molecules which spontaneously and synergistically combine to accomplish certain tasks. As life evolved, the sophistication of these interactions also increased. Organisms evolved by linking the needed functional groups together in proteins to improve the efficiency of the process, and now rely almost exclusively on protein interactions to accomplish needed tasks. It is for this reason that considerable effort has been expended on understanding how such complexes are formed and how the individual components contribute to overall function. The code for these interactions lies buried in the amino acid sequences of the constituent proteins. Biologists are beginning to unravel the secrets of this code, and see how small changes to individual residues can affect the overall stability and function of the complex.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 330: Symposium S – Biomolecular Materials by Design , 1993 , 61
Copyright
Copyright © Materials Research Society 1994

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References

REFERENCES

1) Harrison, P.M., et al. in “Biomineralization: Chemical and Biological Perspectives”, Mann, S., Webb, J., and R.J.P. Williams Eds., VCH Press, Weinheim FRG, 1989, pg. 257.Google Scholar
2) Arosio, P. Adelman, T.G., and Drysdale, J.W. J. Biol. Chem., 253, 4451 (1978).CrossRefGoogle Scholar
3) Cazzola, M. et al., Blood, 62, 1078 (1983).CrossRefGoogle Scholar
4) Rice, D.W., Ford, G.C., White, J.L., Smith, J.M.A., and Harrison, P.M., Adv. Inorganic Biochem., 5, 39 (1983).Google Scholar
5) Harrison., P.M. J. Mol. Biol., 1, 69 (1959).CrossRefGoogle Scholar
6) Gerl, M., and Jaenicke, R., Eur. Biophys., 15, 103 (1987).CrossRefGoogle Scholar
7) Gerl, M., and Jaenicke, R., Biochemistry, 27, 4089, (1988).CrossRefGoogle Scholar
8) Mann, S., et al., Science, 261, 1286 (1993).CrossRefGoogle Scholar
9) Steinart, P.M., and Roop, D.R., Ann. Rev. Biochem., 57, 593 (1988).CrossRefGoogle Scholar
10) Steinart, P.M., et al., Cold Spring Harbor Symp. Quant. Biol., 46, 465 (1982).CrossRefGoogle Scholar
11) Osborn, M., and Weber, K., Lab. Invest., 48, 372 (1983).Google Scholar
12) Herrling, J., and Sparrow, L.G., Int. J. Biol. Macromol., 13, 115 (1991).CrossRefGoogle Scholar
13) O'Shea, E.K., Rutkowski, R., and Kim, P.S., Cell, 66, 699 (1992).CrossRefGoogle Scholar
14) McGrath, K.P., and Kaplan, D.L., MRS Symp. Proc., 292, 83 (1993).CrossRefGoogle Scholar
15) O'Shea, E.K., Lumb, K.J., and Kim, P.S., Current Biology, (in press).Google Scholar
16) McGrath, K.P., DiGirolamo, C.M., and Kaplan, D.L., manuscript in preparation.Google Scholar
17) Jarrett, J.T., and Lansbury, P. T Biochemistry, 31, 12345, (1992).CrossRefGoogle Scholar
18) Zhang, S., Holmes, T., Lockshin, C., and Rich, A., Proc. Natl. Acad. Sci. (USA), 90, 3334(1993).CrossRefGoogle Scholar
19) O'Brien, J. P. et al., In Silk Polymers: Materials Science and Biotechnology, ACS Symp Series, 544, in press (1993).Google Scholar