Wrong ideas have contributed to the development of science in very significant ways. Take, for instance, the cyclol hypothesis. Dorothy Wrinch, a mathematician by training, has been the main proponent of this idea and advanced it rather ferociously. The book “I Died for Beauty” is a fascinating read. The centerpiece of Wrinch’s theory posits that protein folding results from covalent collapse of amides to generate cyclol-dominated structures. Below you can see a protein that has “folded” by way of cyclol formation (now all amide carbons are in their sp3 state). By the way, Dorothy Wrinch was a mathematician, which goes to show that one might want to be skeptical about a mathematiciain’s hypotheses related to chemical bonding, no matter how celebrated that person is. Indeed, any undergraduate chemistry student with knowledge of amino acid side chains should be able to run a “gedanken” (or “thought”) experiment and convince him/herself that it is not feasible to pack amino acid side chains according to the cyclol view of the world. But the theory had persisted until it was eventually discredited by Linus Pauling. While the cyclol idea was shown to be fundamentally wrong, its rejection had an enormous contribution to the discovery of hydrophobic effect. You can read about this in an excellent historical overview (see the link below).
Here is another twist: think about the green fluorescent protein (GFP). Maturation of its chromophore is due to a complicated cascade reaction that starts off a cyclol structure. Take a look below at how this happens. While here there are no multiple cyclol units similar to Wrinch’s folding idea, it is interesting that a significant protein (GFP) owes its function to a structure that has been forged through a covalent bond between two nearby amides. I think we should always remember Dorothy Wrinch!