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Title |
Aromatic-aromatic interactions in structures of proteins and protein-DNA complexes: a study based on orientation and distance |
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Authors |
Ramnath Anjana, Marthandan Kirti Vaishnavi, Durairaj Sherlin, Surapaneni Pavan Kumar, Kora Naveen, Pasam Sandeep Kanth & Kanagaraj Sekar* |
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Affiliation |
Supercomputer Education and Research Centre, Indian Institute of Science, Bangalore 560012, India.
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sekar@physics.iisc.ernet.in; *Corresponding author
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Article Type |
Hypothesis
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Date |
Received November 22, 2012; Accepted November 24, 2012; Published December 08, 2012 |
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Abstract |
Interactions between the aromatic amino acid residues have a significant influence on the protein structures and protein-DNA complexes. These interactions individually provide little stability to the structure; however, together they contribute significantly to the conformational stability of the protein structure. In this study, we focus on the four aromatic amino acid residues and their interactions with one another and their individual interactions with the four nucleotide bases. These are analyzed in order to determine the extent to which their orientation and the number of interactions contribute to the protein and protein-DNA complex structures.
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Citation |
Anjana et al.
Bioinformation 8(24): 1220-1224 (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. |