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Title |
Arginine and Lysine interactions with p residues in metalloproteins |
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Authors |
Parimelzaghan Anitha, Vaideeswaran Sivasakthi, Pandian Lavanya, Susmita Bag, Kalavathi Murugan Kumar, Anand Anbarasu & Sudha Ramaiah* |
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Affiliation |
Bioinformatics Division, School of Biosciences & Technology, VIT University, Vellore-632014, India.
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sudhaanand@vit.ac.in; *Corresponding author
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Article Type |
Hypothesis
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Date |
Received August 18, 2012; Accepted August 20, 2012; Published September 11, 2012
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Abstract |
Metalloproteins have many different functions in cells such as enzymes; signal transduction, transport and storage proteins. About one third of all proteins require metals to carry out their functions. In the present study we have analyzed the roles played by Arg and Lys (cationic side chains) interactions with p (Phe, Tyr or Trp) residues and their role in the structural stability of metalloproteins. These interactions might play an important role in the global conformational stability in metalloproteins. In spite of its lower natural occurrence (1.76%) the number of Trp residues involved in energetically significant interactions is higher in metalloproteins.
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Keywords |
Metalloproteins, p interactions, Arginine, Lysine, sequential distance
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Citation |
Anitha et al.
Bioinformation 8(17): 820-826 (2012) |
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Edited by |
P Kangueane
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ISSN |
0973-2063
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Publisher |
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License |
This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License. |