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Structural features that distinguish kinetically distinct biomineralization polypeptides.
Biomacromolecules
May 2007
Center for Biomolecular Materials Spectroscopy, Laboratory for Chemical Physics, New York University, 345 East 24th Street, New York, New York 10010, USA.
AP7 and AP24 are mollusk shell proteins which are responsible for aragonite polymorph formation and stabilization within the nacre layer of the Pacific red abalone, Haliotis rufescens. It is known that the 30-AA N-terminal mineral modification domains of both proteins (AP7N, AP24N) possess identical multifunctional mineralization capabilities within in vitro assays but differ in terms of rate kinetics, with AP24N > AP7N. In this report, we identify previously unreported molecular features of AP24N and contrast the lowest energy polypeptide backbone structures of AP24N (planar configuration) with that of AP7N ("bent paper clip" configuration) using NMR data and simulated annealing molecular dynamics structure refinement.
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