Abstract
Enzymatic catalysis and reversible binding of external compounds by globular proteins takes either place on the surface of a single or between several rigid β-pleated sheets [1] or, more common, in surface clefts between helices with a width of a few Ångströms. The best known examples are lysozyme, which catalyzes the hydrolysis of poly(acetals) and myoglobin, which binds oxygen [2]. In both cases the clefts are open to the bulk water phase, but nevertheless contain quite a number of hydrophobic amino acids. Furthermore the gap is rigid with well-defined widths and contractions at binding sites. This rigidity is obtained by helical substructures of the protein, to which the active side-chains are bound. As an example, myoglobin [2] and a model peptide containing heme [3] are reproduced in Figure 1. The porphyrin is fixated by two histidine units which bind to the central iron atom and the hydrophobicity of the myoglobin pocket allows for reversible oxygen addition. From the model structure the alternation of rigid binding sites and empty space for the addition of substrates becomes obvious (Figure 1).
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Ruhlmann, L., Zimmermann, J., Messerschmidt, C., Fudickar, W., Fuhrhop, JH. (1999). Rigid Ångström Clefts in Lipid Membranes on Solid Surfaces. In: Ungaro, R., Dalcanale, E. (eds) Supramolecular Science: Where It Is and Where It Is Going. NATO ASI Series, vol 527. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4554-1_13
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DOI: https://doi.org/10.1007/978-94-011-4554-1_13
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