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Diversity of Molecular Recognition: The Combining Sites of Monoclonal Anti Spin Label Antibodies

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NMR in the Life Sciences

Part of the book series: NATO ASI Series ((NSSA,volume 107))

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Abstract

Physical chemistry includes the study of how atoms come together to form molecules, and how combinations of molecules can interact with one another to form aggregates, crystals, and macromolecules. One of the most challenging problems in the area of macromolecules is the problem of protein structure, the problem of finding the “code” that specifies how a given amino acid sequence gives rise to a three-dimensional protein structure, such as an enzyme, with a highly specific biochemical function. This problem has been already attacked with considerable success using NMR methods, through studies of the folding-unfolding of polypeptides and proteins.1 Another important facet of the problem of protein structure, and the evolution of protein structures, concerns the manner in which amino acid sequences corresponding to exons, are assembled as structural units (“modules”) to form three-dimensional structures with specific functions.2

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References

  1. K. R. Shoemaker, P. S. Kim, D. N. Brems, S. Marqusee, E. J. York, I. M. Chaiken, J. M. Stewart, and R. L. Baldwin. Proc. Nat. Acad. Sci. USA 82, 2349–2353 (1985).

    Article  PubMed  CAS  Google Scholar 

  2. W. Gilbert. Science 228, 823–824 (1985) and references therein.

    Article  PubMed  CAS  Google Scholar 

  3. G. M. Griffith, C. Beretz, M. Karartinen and C. Milstein. Nature 312, 271–275 (1984).

    Article  Google Scholar 

  4. G. Kohler and C. Milstein. Nature 256, 495- (1975).

    Article  PubMed  CAS  Google Scholar 

  5. D. R. Davies and H. Metzger. Ann. Rev. Immun, 1, 87–117 (1983).

    Article  CAS  Google Scholar 

  6. L. M. Amzel and R. J. Poljak. Ann. Rev. Biochem. 48, 961–997 (1979).

    Article  PubMed  CAS  Google Scholar 

  7. R. A. Dwek, S. Wain-Hobson, D. Dower, P. Gettins, B. Sutton, J. Perkins and D. Givol. Nature 266, 31–37 (1977).

    Article  PubMed  CAS  Google Scholar 

  8. A. M. Goetze and J. H. Richards. Biochem. 17, 1733–1739 (1978).

    Article  CAS  Google Scholar 

  9. T. Honjo. Ann. Rev. Immun. 1, 499 (1983).

    Article  CAS  Google Scholar 

  10. K. Balakrishnan, F. J. Hsu, D. G. Hafeman and H. M. McConnell, BBA 721, 30–38 (1982).

    PubMed  CAS  Google Scholar 

  11. J. Anglister, T. Frey and H. M. McConnell. Biochem. 23, 1138–1142 (1984).

    Article  CAS  Google Scholar 

  12. T. Frey, J. Anglister and H. M. McConnell. Biochem. 23, 6470–6474 (1984).

    Article  CAS  Google Scholar 

  13. J. Anglister, T. Frey and H. M. McConnell. Nature 315, 65–67 (1985).

    Article  PubMed  CAS  Google Scholar 

  14. J. Anglister, T. Frey and H. M. McConnell. Biochem. 23, 5372–5375 (1984).

    Article  CAS  Google Scholar 

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© 1986 Plenum Press, New York

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McConnell, H.M., Frey, T., Anglister, J., Whittaker, M. (1986). Diversity of Molecular Recognition: The Combining Sites of Monoclonal Anti Spin Label Antibodies. In: Bradbury, E.M., Nicolini, C. (eds) NMR in the Life Sciences. NATO ASI Series, vol 107. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-8178-5_7

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  • DOI: https://doi.org/10.1007/978-1-4684-8178-5_7

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-8180-8

  • Online ISBN: 978-1-4684-8178-5

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