Abstract
Except for the holoproteins that are coloured, because they have small coloured molecules, chromophores, bound to them, proteins are colourless. Many proteins are assemblies of identical subunits and many are assemblies of different (often similar) subunits related by symmetry axes. Beyond the aesthetics of multi-subunit proteins and the aid they provide in structure solution these molecules have physiological advantages. The kinetics of multi-subunit proteins in binding of small molecules shows cooperative binding curves. Of the attempts to explain this phenomenon, the one known as allostery, or MWC model, has enriched biochemistry by offering new terms for describing this phenomenon and its structural consequences. It grew out from the interaction between Jacques Monod, a biochemist and Jefferies Wyman, an uncontested master of the properties of haemoglobin. Beyond providing an explanation of oxygen binding to haemoglobin its success was proven in the study of the kinetics and the conformations of aspartate transcarbamylase.
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Yariv, J. (2016). The Secret of Protein Sophistication. In: The Discreet Charm of Protein Binding Sites. Springer, Cham. https://doi.org/10.1007/978-3-319-24996-4_4
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DOI: https://doi.org/10.1007/978-3-319-24996-4_4
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