Many monomeric proteins can be split into two fragments, yet the two fragments can associate to make an active heterodimer.
To circumvent this drawback, a split aptamer strategy was recently developed, in which nucleic acid aptamers were split into two fragments that could specifically form a ternary assembly in the presence of ligand.
When a neutron strikes the nucleus of an atom of the isotopes uranium-235 or plutonium-239, it causes that nucleus to split into two fragments, each of which is a nucleus with about half the protons and neutrons of the original nucleus.
To construct the aptasensor, the sequence of the 15-base anti-thrombin DNA aptamer was split into two fragments, one of which was attached to a gold electrode via thiol self-assembled monolayer chemistry and the second of which was modified with the redox moiety ferrocene.
An intein domain is split into two fragments, IntN and IntC, which are fused to the flanking exteins, ExN and ExC.
An intein domain is split into two fragments (split intein or trans-splicing intein), IntN and IntC, which are fused to the flanking polypeptides, termed the N and C exteins (ExN and ExC).
On the other hand, Roszak and Weaver [10] summarized that the hydantoin ring structure can be split into two fragments, one responsible for the anticonvulsant activity N3-C4 =O -C55) and the other for mutagenic effects (-C2 =O -N3(H)).
In this method a fluorescent protein such as CFP is split into two fragments, and then fused to proteins of interest.
The 417 base pairs (bp) product was cut into three fragments of 188, 186, and 43 bp for the 5178C polymorphism, whereas it was split into two fragments of 374 and 43 bp for the 5178A polymorphism.
