作者: Asiya Gul , Peter Rez
DOI: 10.1007/S00240-007-0087-3
关键词:
摘要: It is widely believed that proteins rich in Asp, Glu or Gla (gamma carboxyglutamic acid) interact strongly with calcium oxalate surfaces and inhibit crystal growth. An alternative hypothesis would be the interaction of residues could facilitate nucleation aggregation. Prothrombin fragment 1 bikunin have been studied extensively as inhibitors, beta-microglobulin, transferrin antitrypsin found stone matrix tubulin has observed attachment crystals to cell surfaces. The aim this study examine how well carboxylate groups either matrix, proposed fit ion sub-lattice both monohydrate dihydrate acidic were marked Protein Data Bank structures matched using Cerius 3D molecular modeling program. A contact was defined if a oxygen atom approached surface such way separation less than 6 Angstrom but greater 2.4 Angstrom, sum ionic radii. If maintain their structure, number contacts no more 3 4 for all studied, irrespective surface.