Abstract
Effective molecular recognition requires the precise alignment of binding groups on the receptor with chemical features on the substrate. In the past two years we have initiated a program aimed at the development of artificial receptors containing several recognition sites that are complementary with biologically-interesting molecules. This project was inspired by a lecture at the 4th IPMR in Lancaster by Professor W. Saenger in which he discussed the X-ray structure of the guanine-binding enzyme, ribonuclease T1 [1]. This shows a guanine substrate bound into the active site by both hydrogen bonding to the peptide backbone and aromatic stacking to a tyrosine aromatic ring (Figure 1). The presence of two recognition interactions increases both the strength and specificity of substrate binding.
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References
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© 1990 Plenum Press, New York
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Hamilton, A.D. (1990). Molecular Recognition by Macrocyclic Receptors. In: Atwood, J.L. (eds) Inclusion Phenomena and Molecular Recognition. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0603-0_6
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DOI: https://doi.org/10.1007/978-1-4613-0603-0_6
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