Proton assignment and structural features of a peptide from the chymosin-sensitive region of bovine k-casein determined by 2D-NMR spectroscopy

✍ Scribed by Jeffrey E. Plowman; Mark H. Smith; Lawrence K. Creamer; Michael J. Liddell; Jan M. Coddington; Jennifer J. Gibson; Darren R. Engelbretsen

• Publisher: John Wiley and Sons
• Year: 1994
• Tongue: English
• Weight: 682 KB
• Volume: 32
• Category: Article
• ISSN: 0749-1581
• DOI: 10.1002/mrc.1260320805

✦ Synopsis

Abstract

The peptide k‐casein(98–111) corresponding to the sequence 98–111 of bovine k‐casein (His‐Pro‐His‐Pro‐His‐Leu‐Ser‐Phe‐Met‐Ala‐Ile‐Pro‐Pro‐Lys), which includes the aspartic protease sensitive region, was analysed by 2D ^1^H NMR spectroscopic techniques in DMSO‐d~6~. The spectral peaks of all protons resolved at 400 MHz were assigned. The changes in the amide proton shifts with pH and temperature and the existence of particular cross peaks in the ROESY spectra were consistent with the central region of the peptide being in an extended chain in solution but with some type of distinct conformations at the N‐ and C‐termini. The results are not consistent with the peptide having any helical structure at either low or high pH.