1996-2019 All Rights Reserved. Online Journal of Bioinformatics . You may not store these pages in any form except for your own personal use. All other usage or distribution is illegal under international copyright treaties. Permission to use any of these pages in any other way besides the  before mentioned must be gained in writing from the publisher. This article is exclusively copyrighted in its entirety to OJB publications. This article may be copied once but may not be, reproduced or  re-transmitted without the express permission of the editors. This journal satisfies the refereeing requirements (DEST) for the Higher Education Research Data Collection (Australia). Linking:To link to this page or any pages linking to this page you must link directly to this page only here rather than put up your own page.



 Online Journal of Bioinformatics  


Volume 9 (2): 92-107, 2008.

In-silico study on interaction of active binding sites of proteins with calcium oxalate monohydrate


Bijarnia RK1, Kaur T, Naik PK1, Singla SK2, Tandon C1


1Department of Biotechnology and Bioinformatics, Jaypee University of Information Technology, Waknaghat, Solan and 2Department of Biochemistry, Punjab University, Chandigarh, India.




Bijarnia RK, Kaur T, Naik PK,  Singla SK, Tandon C., In-silico interaction of active binding sites of proteins with calcium oxalate monohydrate, Online J Bioinformatics, 9 (2):92-107, 2008  The In silico interaction of calcium oxalate monohydrate (COM) with active protein binding sites of  bikunin, osteonectin, urinary prothrombin, CD59 and MAp19 is described. Active binding sites were predicted and binding affinity with COM was estimated using Molecular Operation Environment software. Results showed that carboxyl and hydroxyl amino acids bonded strongly with the calcium ion of COM. The findings suggest that acidic amino acids bond strongly with COM and the presence of other amino acids further strengthens bonding.


Keywords: calcium oxalate monohydrate (COM), crystallization, hydrogen bonding, hydrophophic interactions, inhibitory protein, kidney stone.