Abstract
Non-covalent bonding (e.g. electrostatic or ionic, hydrophobic and hydrogen bonding) is very important in maintaining the intra- and intermolecular interactions critical to the functioning of biological macromolecules in aqueous environments. The three-dimensional structure compatible with these functional interactions is stabilized in most enzymes by covalent non-peptide (e.g. disulfide) bonds. The introduction of additional covalent bonds within and between enzyme molecules thus seems to be a reasonable approach to the stabilization of the functional interactions for their subsequent study and use in unnatural environments.
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Guire, P. (1978). Stepwise Thermophotochemical Crosslinking for Enzyme Stabilization and Immobilization. In: Pye, E.K., Weetall, H.H. (eds) Enzyme Engineering. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-5163-5_8
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DOI: https://doi.org/10.1007/978-1-4757-5163-5_8
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