Secondary structure prediction of human salivary proline‐rich proteins

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Abstract
Conformations associated with secondary structure in human salivary proline-rich proteins A (PRPA), C (PRPC), P-D and P-E were predicted by analysis of their respective hydrophobicity profiles by computer programming. Structurally, PRPA and PRPC would present a globular head and a tail that consists of type 310 polyproline helices. P-D and P-E would be fibrilar molecules with helical zones of the polyproline 310 type. Alternatively for PRPA and PRPC, the head and tail would form one globular domain with the tail folding upon itself at places where random coils occur.