Wrinch developed this suggestion into a full-fledged model of protein structure. The basic cyclol model was laid out in her first paper (1936). She noted the possibility that polypeptides might cyclize to form closed rings (true) and that these rings might form internal crosslinks through the cyclol reaction (also true, although rare). Assuming that the cyclol form of the peptide bond could be more stable than the amide form, Wrinch concluded that certain cyclic peptides would naturally make the maximal number of cyclol bonds (such as cyclol 6, Figure 2). Such cyclol molecules would have hexagonal symmetry, if the chemical bonds were taken as having the same length, roughly 1.5 Å; for comparison, the N-C and C-C bonds have the lengths 1.42 Å and 1.54 Å, respectively.
These rings can be extended indefinitely to form a cyclol fabric (Figure 3). Such fabrics exhibit a long-range, quasi-crystalline order that Wrinch felt was likely in proteins, since they must pack hundreds of residues densely. Another interesting feature of such molecules and fabrics is that their amino-acid side chains point axially upwards from only one face; the opposite face has no side chains. Thus, one face is completely independent of the primary sequence of the peptide, which Wrinch conjectured might account for sequence-independent properties of proteins.
In her initial article, Wrinch stated clearly that the cyclol model was merely a working hypothesis, a potentially valid model of proteins that would have to be checked. Her goals in this article and its successors were to propose a well-defined testable model, to work out the consequences of its assumptions and to make predictions that could be tested experimentally. In these goals, she succeeded; however, within a few years, experiments and further modeling showed that the cyclol hypothesis was untenable as a model for globular proteins.