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• W2022306116 abstract "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 1 H NMR assignment was performed for the peptide at three Ca 2+ 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 Leu 16 and Asn 27 adopted conformations with an increased contribution of α-helical structure, a so-called nascent helix. Two regions, Glu 11 -SerP 15 and Lys 29 -Phe 33 showed an increased population of conformations with extended structures. Addition of Ca 2+ 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 Ca 2+ stabilized the structure already present in the apo form of the peptide." @default.
• W2022306116 created "2016-06-24" @default.
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• W2022306116 date "1994-11-01" @default.
• W2022306116 modified "2023-10-01" @default.
• W2022306116 title "Secondary structures in β-casein peptide 1–42: a two dimensional nuclear magnetic resonance study" @default.
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• W2022306116 doi "https://doi.org/10.1017/s0022029900028429" @default.
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