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[Play Now]( Mandarin Palace Casino | [Live Chat]( | [Contact us]( | [Unsubscribe]( Dear fgVvWCmq fgVvWCmq, Welcome to the Enterprise Plus® membership experience. The oxygen-transporting protein haemoglobin has under gone repeated adaptations as animals evolved to conquer new environments — from the depths of the oceans1 to high mountain ranges2. These adaptations relied on changes in the long-range interactions between oxygen-binding sites buried in the protein’s subunits, and between these regions and binding sites for a multitude of small effector molecules on the protein’s surface3. How did this complex molecular machine, which can respond so exquisitely to available levels of both oxygen and several other effector molecules, come into being? Writing in Nature, Pillai et al.4 reconstruct the stepwise evolution of haemoglobin from precursors that existed more than 400 million years ago. =========== Almost nothing was previously known about how the four-subunit (tetrameric) form of haemoglobin that is found in modern-day jawed vertebrates evolved from ancient monomers. Tetrameric haemoglobin consists of two α- and two β-subunits. Pillai et al. computationally reconstructed an evolutionary tree to chart the protein’s ancient history, using the amino-acid sequences of a large collection of the closely related vertebrate globin proteins, which exist as either monomers or tetramers. The authors’ tree was constructed taking into account that amino-acid substitutions a given protein shares with close relatives tend to have originated in more-recent common ancestors than have those it shares with more-distant relatives. The reconstructed evolutionary tree indicates that multiple rounds of gene duplication and subsequent divergence gave rise to the globin family and, by way of several ancestral proteins, to tetrameric haemoglobin (Fig. 1). A lens combined with an artificial iris is placed at the front of the device, just as in the human eye. The retina at the back combines with a hemispherical shell at the front to form a spherical chamber (the ‘eyeball’); the frontal hemispherical shell is made from aluminium lined with a tungsten film. The chamber is filled with an ionic liquid that mimics the vitreous humour — the gel that fills the space between the lens and the retina in the human eye. This arrangement is necessary for the electrochemical operation of the nanowires. The overall structural similarity between the artificial eye and the human eye confers on Gu and colleagues’ device a wide field of view of 100°. This compares with roughly 130° for the vertical field of view of a static human eye. 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