Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 495-506 |
| Number of pages | 12 |
| Journal | Journal of Dairy Research |
| Volume | 61 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 1994 |
| MoE publication type | A1 Journal article-refereed |
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Secondary structures in β-casein peptide 1–42 : A two dimensional nuclear magnetic resonance study. / Wahlgren, M.; Dejmek, P.; Drakenberg, Torbjörn.
In: Journal of Dairy Research, Vol. 61, No. 4, 1994, p. 495-506.Research output: Contribution to journal › Article › Scientific › peer-review
TY - JOUR
T1 - Secondary structures in β-casein peptide 1–42
T2 - A two dimensional nuclear magnetic resonance study
AU - Wahlgren, M.
AU - Dejmek, P.
AU - Drakenberg, Torbjörn
PY - 1994
Y1 - 1994
N2 - Two dimensional NMR spectroscopy was used to study the structure of a peptide composed of the N-terminal 42 amino acid residues of beta-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 alpha-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 alpha-helical structure, indicating that the addition of Ca2+ stabilized the structure already present in the apo form of the peptide.
AB - Two dimensional NMR spectroscopy was used to study the structure of a peptide composed of the N-terminal 42 amino acid residues of beta-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 alpha-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 alpha-helical structure, indicating that the addition of Ca2+ stabilized the structure already present in the apo form of the peptide.
U2 - 10.1017/S0022029900028429
DO - 10.1017/S0022029900028429
M3 - Article
VL - 61
SP - 495
EP - 506
JO - Journal of Dairy Research
JF - Journal of Dairy Research
SN - 0022-0299
IS - 4
ER -