Secondary structure prediction of human salivary proline‐rich proteins

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.