Secondary structure prediction of human salivary proline‐rich proteins

FEBS Letters

Vargas, Veronica²  Cid, Hilda²  Bunster, Marta²  Bustos, Sergio¹ 

[1] Department of Oral Biology-Biochemistry, Medical College of Georgia, Augusta, GA 30912, USA;>Department of Molecular Biology, Faculty of Biological Sciences and Natural Resources, University of Concepcion, Concepcion, Chile

关键词: Proline-rich protein;    Conformation;    Computer prediction;    Sequence homology;    Structural model (Human saliva);   

DOI  :  10.1016/0014-5793(86)81200-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown