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

M. Wahlgren, P. Dejmek, Torbjörn Drakenberg

Research output: Contribution to journalArticleScientificpeer-review

22 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)495-506
Number of pages12
JournalJournal of Dairy Research
Volume61
Issue number4
DOIs
Publication statusPublished - 1994
MoE publication typeA1 Journal article-refereed

Fingerprint

Caseins
nuclear magnetic resonance spectroscopy
casein
Magnetic Resonance Spectroscopy
peptides
Peptides
endoproteinase Asp-N
calcium
Phosphoserine
beta-casein
amides
Amides
protons
Protons
Amino Acids
amino acids
Population

Cite this

Wahlgren, M. ; Dejmek, P. ; Drakenberg, Torbjörn. / Secondary structures in β-casein peptide 1–42 : A two dimensional nuclear magnetic resonance study. In: Journal of Dairy Research. 1994 ; Vol. 61, No. 4. pp. 495-506.
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abstract = "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.",
author = "M. Wahlgren and P. Dejmek and Torbj{\"o}rn Drakenberg",
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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 journalArticleScientificpeer-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 -