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Lise R. L. Pedersen, Søren B. Nielsen, Jon G. Hansted, Torben E. Petersen, Daniel E. Otzen and Esben S. Sørensen PP3 forms stable tetrameric structures through hydrophobic interactions via the C-terminal amphipathic helix and undergoes reversible thermal dissociation and denaturation The FEBS Journal 279

Version of Record online: 6 DEC 2011 | DOI: 10.1111/j.1742-4658.2011.08428.x

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The milk protein proteose peptone component 3 (PP3), also called lactophorin, forms stable well-defined multimeric structures. The monomers associate to tetramers through hydrophobic interactions via the hydrophobic surface of the C-terminal amphipathic α-helices. The study suggests that PP3 tetramers act as reservoirs of PP3 molecules, which in the monomeric state may stabilize the milk fat globule.

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