4ck4

Publication Abstract from PubMed

The crystal structure of the triclinic form of the milk protein beta-lactoglobulin from sheep (Ovis aries) at 1.1 A 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.

Ovine beta-lactoglobulin at atomic resolution.,Kontopidis G, Nordle Gilliver A, Sawyer L Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1498-503. doi:, 10.1107/S2053230X14020950. Epub 2014 Oct 31. PMID:25372816^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.