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One of the important issues in molecular biology is the three-dimensional structure (shape) of proteins and their precursors (deoxyribonucleic acid (DNA) and ribonucleic acid (RNA)) in the cell, and the close relationship between macromolecular structure and function. Ordinarily, protein and DNA structure is determined by X-ray crystallography, electron and atomic force microscopy, and nuclear magnetic resonance imaging (NMR). Because of the close packing needed for crystallization, the manipulation required to prepare a specimen for electron or atomic force microscopy, and the lack of resolution of NMR, these methods often do not provide conclusive evidence for molecular shape in solution. Moreover, some proteins (enzymes) function as molecular machines, changing their shape as they execute their function, so one static spatial snapshot may not tell the whole story. Topology can shed light on this key issue. The topological approach to enzymology is an experimental protocol in which the descriptive and analytical powers of topology and geometry are employed in an indirect effort to determine enzyme mechanism and the structure of active enzyme-DNA complexes in vitro (in a test tube) and in vivo (in the cell). It is possible to use a three-component field with a fixed magnitude and a lagrangian with two terms to construct a knot in field theory. Recent research has developed twists and linkings in string to produce two forms of stable knot, known as trefoils and unknots. It has been shown that these finite loops of string do not contract or dissipate, and are therefore lump solitons. It will be particularly interesting to look at how these knot configurations withstand perturbations.