This covalent attachment of ubiquitin or ubiquitin-like proteins to targeted proteins is a major mechanism for regulating protein function in eukaryotic organisms.

On the other end of the tRNA is a covalent attachment to the amino acid that corresponds to the anticodon sequence.

The ability for them to build off of electrode surfaces is likely to be an electrostatic interaction, while on other surfaces covalent attachment is possible.

(In contrast, it is the labile thiol ester that permits covalent attachment between C3 and nucleophilic acceptors.)

In most gram-positive bacteria, certain proteins are targeted for export across the plasma membrane and subsequent covalent attachment to the bacterial cell wall.

Improvement in the mucoadhesive properties of alginate by the covalent attachment of cysteine.

Similar to silicon, the surface of mica does not contain an appreciable density of silanol groups for covalent attachment by silanes.

The covalent attachment of ubiquitin inactivates D2 by disrupting dimerization and targets it to degradation in the proteosome.

These reactions involve covalent attachment of small polar endogenous molecule such as glucuronic acid, sulfate, or glycine to form water-soluble compounds.

However, there is no clear evidence that other covalent attachments do not form.