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Issue title: Selected Papers from ICCMEH2014
Guest editors: Raghuvir Pai
Article type: Research Article
Authors: Raju, Deepa K. M. | Ajees, A. Abdul*
Affiliations: Department of Atomic and Molecular Physics, Manipal University, Manipal-576104, Karnataka, India
Correspondence: [*] Corresponding author: A. Abdul Ajees, Department of Atomic and Molecular Physics, Manipal University, Manipal-576104, Karnataka, India. Tel.: +91 8147966458; E-mail:[email protected]
Abstract: The post-genomic era produces an overwhelming amount of experimental data, but majority of such data lacks the characterization of its functions. Structure based approaches are useful to understand and characterize the functional aspects of proteins. Given the burgeoning requirement of understanding the functional aspects of various enzymes, we report a systematic structure based study of methyltransferases bound with S-adenosyl-L-methionine (SAM). Through this work, we identified the conserved amino acids of methyltransferase, which are interacting with SAM.
Keywords: Amino acids, methyltransferase, protein data bank, S-adenosyl-L-methionine
DOI: 10.3233/JCM-170711
Journal: Journal of Computational Methods in Sciences and Engineering, vol. 17, no. 2, pp. 283-287, 2017
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