Secondary structure of bovine alphaS2-casein: theoretical and experimental approaches
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Updated: Oct 4, 2026

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
Published on: April 14, 2015
P D Hoagland1, J J Unruh, E D Wickham
1U. S. Department of Agriculture, Agriculture Research Service, Eastern Regional Research Center, Wyndmoor, PA 19038, USA. phoagland@arserrc.gov
Abstract:
Circular dichroism and Fourier transform infrared spectroscopy of bovine alphaS2-casein both report a 24 to 32% content of alpha-helix. A consensus of sequence based predictions for alpha-helix suggests a Lys77-Gln91 helix within the sequence (Ser61-Arg125). This motif is repeated at (Ser143-Leu207), and this region contains a longer Thr145-Leu177 predicted alpha-helix. A short, seven-member alpha-helix may also organize the N-terminal peptide that precedes the first phosphoserine [-Srp-]3 cluster. As was found for other caseins studied by these spectroscopic methods, a high degree of extended beta-sheet (approximately 30%) and turns (25 to 30%) are predicted for alphaS2-casein.
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