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Ovine β‐lactoglobulin at atomic resolution
Author(s) -
Kontopidis George,
Nordle Gilliver Anna,
Sawyer Lindsay
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14020950
Subject(s) - beta lactoglobulin , chemistry , resolution (logic) , materials science , biophysics , whey protein , food science , biology , computer science , artificial intelligence
The crystal structure of the triclinic form of the milk protein β‐lactoglobulin from sheep ( Ovis aries ) at 1.1 Å resolution is described together with a comparison of the triclinic structures of the low‐pH bovine and high‐pH ovine proteins. All three structures are remarkably similar, despite the well known pH‐dependent conformational transition described for the bovine and porcine proteins that occurs in solution. The high resolution of the present structure determination has allowed a more accurate description of the protein than has hitherto been possible, but it is still not clear whether flexibility changes in the external loops can compensate for the presence of a significant void in the unliganded interior of the structure.