Abstract
Four convex uniform polyhedra were utilized in the consideration of possible models for the arrangement of 24 identical protein subunits to form the shell-like structure of apoferritin. Comparisons between the dimensions of the different models and those reported for apoferritin permitted the elimination of only one model. The properties predicted for each of the models, such as numbers and sizes of dissociation intermediates, numbers and relative sizes of pores, and the symmetries of potential iron binding sites suggest experimental approaches which may be used to elucidate the structure of apoferritin.
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