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Life Sciences

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Published yearly: 

4 Issues


ISSN: 2320-964X (Online) 

ISSN: 2320-7817  (Print)



Dr. Santosh Pawar 




Int. Journal of Life Sciences, 2016; 4(2):185-192 |  Available online,July 23, 2016

S6 peptide derived from KvAP channel shows marked differences in secondary structure after mutation- a computational approach



Chetan Malik1*, Rajan Shrivastava2, Subhendu Ghosh2, Hasan SS1


1Department of Life Science, School of Sciences, Indira Gandhi National Open University, New Delhi, 110068, India

2Department of Biophysics, University of Delhi South Campus, New Delhi, 110021, India

*Corresponding author: Email:  |   Phone +919818994921


Received: 16.05.2016   |    Accepted: 10.06.2016   |   Published : 23.07.2016

KvAP is a widely studied potassium channel from bacterium Aeropyrum pernix. It is composed of six trans-membrane domains ranging from S1 to S6. Out of these six domains, S6 is the domain through which transfer of ions occurs. We have analyzed the structural differences in the s6 domains after mutating more hydrophobic amino acids with less hydrophobic amino acids. The computational studies suggest that there is a change in the secondary structures of protein which leads to its altered functioning. The RMSD (Root mean square distance) of the peptides were calculated and significant differences were observed in Ramachandran plot. The computational analysis complements the earlier published results.


Keywords: KvAP channel, Secondary structure, Ramachandran plot, RMSD (Root Mean Square Deviation), Hydrophobicity.


Editor: Dr. Arvind Chavhan


Cite this article as:

Chetan Malik, Rajan Shrivastava, Subhendu Ghosh, Hasan SS (2016) S6 peptide derived from KvAP channel shows marked differences in secondary structure after mutation- a computational approach, International J. of Life Sciences, 4 (2): 185-192.



Copyright: © 2016 | Author(s), This is an open access article under the terms of the Creative Commons Attribution-Non-Commercial - No Derivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.



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