Unravelling conformational aspects of milk protein structure-contributions from nuclear magnetic resonance studies

Tatijana Markoska, Todor Vasiljevic, Thom Huppertz*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

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 diffcult 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.

Original languageEnglish
Article number9081128
JournalFoods
Volume9
Issue number8
DOIs
Publication statusPublished - Aug 2020

Keywords

  • Casein
  • Milk protein
  • Nmr
  • Protein structure
  • Whey protein

Fingerprint Dive into the research topics of 'Unravelling conformational aspects of milk protein structure-contributions from nuclear magnetic resonance studies'. Together they form a unique fingerprint.

Cite this