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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.