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Review

Unravelling Conformational Aspects of Milk Protein Structure—Contributions from Nuclear Magnetic Resonance Studies

1
Advanced Food Systems Research Unit, Institute for Sustainable Industries and Liveable Cities, College of Health and Biomedicine, Victoria University, Melbourne VIC 8001, Australia
2
FrieslandCampina, 3818 LE Amersfoort, The Netherlands
3
Food Quality and Design Group, Wageningen University and Research, 6808 WG Wageningen, The Netherlands
*
Author to whom correspondence should be addressed.
Foods 2020, 9(8), 1128; https://doi.org/10.3390/foods9081128
Received: 25 July 2020 / Revised: 11 August 2020 / Accepted: 13 August 2020 / Published: 16 August 2020
(This article belongs to the Special Issue Recent Advances and Trends in the Dairy Field)
Changes in the molecular structure and association of milk proteins lead to many desirable (under controlled conditions) or undesirable characteristics of dairy products. Several methods have been used to study the structure of milk proteins and changes therein in different environments. Whey proteins are an excellent model for secondary structure studies using circular dichroism (CD), Fourier-transform infrared spectroscopy (FTIR) and tertiary structure studies using X-ray crystallography and nuclear magnetic resonance (NMR). However, caseins, the most abundant protein class in milk, are far more difficult to characterize. The tertiary structure of caseins cannot be observed by X-ray crystallography due to the inability to crystallize caseins. However, NMR is an appropriate approach for structural elucidation. Thus far, NMR was applied on specific peptides of individual caseins of the molecules including phosphoserine centers and colloidal calcium phosphate. The literature focuses on these parts of the molecule due to its importance in building the sub-unit particles involving individual caseins and calcium phosphate nanoclusters. This review focuses on present structural studies of milk proteins using NMR and their importance in dairy processing. View Full-Text
Keywords: NMR; milk protein; protein structure; casein; whey protein NMR; milk protein; protein structure; casein; whey protein
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MDPI and ACS Style

Markoska, T.; Vasiljevic, T.; Huppertz, T. Unravelling Conformational Aspects of Milk Protein Structure—Contributions from Nuclear Magnetic Resonance Studies. Foods 2020, 9, 1128. https://doi.org/10.3390/foods9081128

AMA Style

Markoska T, Vasiljevic T, Huppertz T. Unravelling Conformational Aspects of Milk Protein Structure—Contributions from Nuclear Magnetic Resonance Studies. Foods. 2020; 9(8):1128. https://doi.org/10.3390/foods9081128

Chicago/Turabian Style

Markoska, Tatijana, Todor Vasiljevic, and Thom Huppertz. 2020. "Unravelling Conformational Aspects of Milk Protein Structure—Contributions from Nuclear Magnetic Resonance Studies" Foods 9, no. 8: 1128. https://doi.org/10.3390/foods9081128

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