Abstract
Macromolecular recognition is a unifying theme in biology and biotechnology and understanding the mechanisms underlying this phenomenon remain important goals of biochemical study. The structural nature of recognition surfaces for an increasing array of macromolecules, especially proteins, can now be described at high resolution thanks largely to diffraction analysis of their crystals. Such protein structures offer an improved opportunity to focus solution biochemical experiments in order to define the forces responsible for their surface interactions and consequent functions. Moreover, improved understanding of protein as well as peptide interactions brings with it the ability increasingly to use these phenomena in technology, for example, as vehicles for separation, enzyme regulation, immunodiagnostics and therapy, the redesign of native macromolecules to produce new functions and the de novo design of non-biological surrogates.
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Chaiken, I.M., Ando, S., Shai, Y., Fassina, G., Liang, X. (1987). Synthetic Peptides and the Design of Peptide and Protein Recognition Surfaces. In: Chaiken, I., Chiancone, E., Fontana, A., Neri, P. (eds) Macromolecular Biorecognition. Experimental Biology and Medicine, vol 19. Humana Press. https://doi.org/10.1007/978-1-4612-4600-8_3
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DOI: https://doi.org/10.1007/978-1-4612-4600-8_3
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