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J. Biochem, 1998, Vol. 123, No. 1 150-156
© 1998 Japanese Biochemical Society

research-article

Small-Angle X-Ray Scattering and Computer-Aided Molecular Modeling Studies of 20 kDa Fragment of Porcine Amelogenin: Does Amelogenin Adopt an Elongated Bundle Structure?1

Norio Matsushima*,2, Yoshinobu Izumi{dagger} and Takaaki Aoba{ddagger}

*School of Health Sciences, Sapporo Medical University Chuo-ku, Sapporo 060
{dagger}Graduate School of Engineering, Yamagata University Yamagata 992
{ddagger}Department of Pathology, Faculty of Dentistry, Nippon Dentistry University Chiyoda-ku, Tokyo 102

2To whom correspondence should be addressed. Tel: +81-11-611-2111, Fax: -81-11-613-7134, E-mail: matusima{at}shs.sapmed.ac.jp

Amelogenins, which are major matrix constituents in the developing tooth, play a regulatory role in the process of enamel crystal formation. Porcine amelogenin with 173 amino acid residues is rich in proline, glutamine, leucine, and histidine. We utilized the smallangle X-ray scattering (SAXS) technique to examine the solution structure of porcine amelogenin. Samples used were two porcine amelogenins with apparent molecular weights of 20 kDa (amino acids 1 to 148) and 13 kDa (amino acids 46 to 148) on SDS-PAGE. Prior to SAXS measurements, the protein samples were dissolved in 2% (v/v) acetic acid to give a concentration range up to 10 mg/ml. Comparison between Rc (the overall radius of gyration) and Rg (the cross-sectional radius of gyration) revealed that the 20 kDa amelogenin exists in this solution as asymmetric particles with a length of about 15 nm, presumably corresponding of dimers. Based on these experimental data and computeraided molecular modeling studies, we propose that the 20 kDa amelogenin adopts an elongated bundle structure which mainly consists of extended structures similar to polyproline II and/or ß-strand, interspersed with ß-turn or loop.

1This work has been performed with the approval of the Photon Factory Advisory Committee (Proposal No. 95G089).


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H.C. Margolis, E. Beniash, and C.E. Fowler
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