In the early 1970's, crystallographer Byron Rubin invented a tool that bends wires to make proteins models. The tool was popular until the 1990s. Byron Rubin became an artist who builds large-scale molecular sculptures.
Eric Martz and Eric Francoeur explain how such physical models yielded important scientific insights:
An example illustrating the importance of models from Byron's Bender occurred at a scientific meeting in the mid 1970's. At this time, less than two dozen protein structures had been solved. David Davies brought a Bender model of an immunoglobulin Fab fragment, and Jane and David Richardson brought a Bender model of superoxide dismutase. While comparing these physical models at the meeting, they realized that both proteins use a similar fold, despite having only about 9% sequence identity. This incident was the first recognition of the occurrence of what is now recognized as the immunoglobulin superfamily domain in proteins that are apparently unrelated by sequence. The insight was published in a paper entitled "Similarity of three-dimensional structure between the immunoglobulin domain and the copper, zinc superoxide dismutase subunit" ( Richardson et al., J. Mol. Biol. 102:221-235, 1976).
Also see the more recent DIWire device by Pensalabs.
Sources:
- Byron Rubin. molecularsculpture.com.
- Eric Martz and Eric Francoeur (1997-2004) History of Visualization of Biological Macromolecules.
- Left image from molecularsculpture.com. Right image from The Journal of Biocommunication.