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Secondary structures in β-casein peptide 1–42: a two dimensional nuclear magnetic resonance study

Published online by Cambridge University Press:  01 June 2009

N. Magnus Wahlgren ,
Petr Dejmek  and
Torbjörn Drakenberg
N. Magnus Wahlgren
Affiliation:
Department of Food Technology, University of Lund, PO Box 124, S-221 00 Lund, Sweden Department of Physical Chemistry 2, University of Lund, PO Box 124, S-221 00 Lund, Sweden
Petr Dejmek
Affiliation:
Department of Food Engineering, University of Lund, PO Box 124, S-221 00 Lund, Sweden
Torbjörn Drakenberg
Affiliation:
Department of Physical Chemistry 2, University of Lund, PO Box 124, S-221 00 Lund, Sweden Chemical Laboratory, The Technical Research Center of Finland, PO Box 204, SF-0 2151, Finland
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Summary

Two dimensional NMR spectroscopy was used to study the structure of a peptide composed of the N-terminal 42 amino acid residues of β-casein. The peptide was obtained by enzymic cleavage using endoproteinase Asp-N. Complete sequence-specific 1H NMR assignment was performed for the peptide at three Ca2+ concentrations (0, 22 and 37 mM). The NMR results show that the peptide was highly flexible and adopted multiple conformations. No stable secondary structures were present; however, the peptide had some regions with non-random structure. The region between residues Leu16 and Asn27 adopted conformations with an increased contribution of α-helical structure, a so-called nascent helix. Two regions, Glu11-SerP15 and Lys29-Phe33 showed an increased population of conformations with extended structures. Addition of Ca2+ induced chemical shift changes for the backbone amide protons, especially around the phosphoserine region and around the suggested α-helical structure, indicating that the addition of Ca2+ stabilized the structure already present in the apo form of the peptide.

Type
Original articles
Information
Journal of Dairy Research , Volume 61 , Issue 4 , November 1994 , pp. 495 - 506
Copyright
Copyright © Proprietors of Journal of Dairy Research 1994

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