Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870577 | FEBS Letters | 2014 | 7 Pages |
Abstract
β-Lactoglobulin (βlg) is the most abundant whey protein in the milks of ruminant animals. While bovine βlg has been subjected to a vast array of studies, little is known about the caprine ortholog. We present an ultra-high resolution crystal structure of caprine βlg complemented by analytical ultracentrifugation and small-angle X-ray scattering data. In both solution and crystalline states caprine βlg is dimeric (KD < 5 μM); however, our data suggest a flexible quaternary arrangement of subunits within the dimer. These structural findings will provide insight into relationships among structural, processing, nutritional and immunological characteristics that distinguish cow's and goat's milk.
Keywords
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Authors
Jennifer M. Crowther, Moritz Lassé, Hironori Suzuki, Sarah A. Kessans, Trevor S. Loo, Gillian E. Norris, Alison J. Hodgkinson, Geoffrey B. Jameson, Renwick C.J. Dobson,