Synthesis and circular dichroism study of the human salivary proline‐rich protein IB7 | Zendy

Simon Cécile | Zendy; Pianet Isabelle | Zendy; Dufourc Erick J. | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

Synthesis and circular dichroism study of the human salivary proline‐rich protein IB7

Author(s) -

Simon Cécile,

Pianet Isabelle,

Dufourc Erick J.

Publication year - 2003

Publication title -

journal of peptide science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.475

H-Index - 66

eISSN - 1099-1387

pISSN - 1075-2617

DOI - 10.1002/psc.438

Subject(s) - circular dichroism , chemistry , protein secondary structure , proline , acetic anhydride , amino acid , glycine , glutamine , piperidine , random coil , stereochemistry , biochemistry , catalysis

The solid phase synthesis of a 59 amino acid human salivary protein IB7 has been accomplished using Fmoc strategy. Because the protein contains 25 proline, 13 glycine and 9 glutamine residues the coupling time, piperidine delivery and acetic anhydride reaction time were increased. Yield after HPLC purification was 35%. Circular dichroism studies revealed that about one third of IB7 residues adopted a type II helix secondary structure, as found in collagen helices. The rest of the sequence adopts a random coil secondary structure. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research