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Biochemists made a new molecular design discovery when they mapped for the first time the three-dimensional crystal structure of osteocalcin, the most abundant noncollagenous protein in bone. Their map revealed unique structures in the protein that permit it to recognize, recruit, and bind a key mineral component of bone, namely hydroxyapatite. Thus, osteocalcin joins a growing host of proteins whose 3-D maps reveal design matching the best efforts seen in humanly manufactured machines. Such elegant design is highly improbable in an evolutionary paradigm.
Quyen Q. Hoang, et al, “Bone Recognition Mechanism of Porcine Osteocalcin from Crystal Structure,” Nature, 425 (2003), pp. 977-980.
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