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

Abstract

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.