Abstract
Sequence analysis is a computational biology method to study protein sequences by comparing amino acids of one protein sequence with the other (residual level comparison). This study reveals a new concept of comparing protein sequences at their basic atomic level. Aquaporins from various origin were compared at their atomic level and the study revealed that all the aquaporin proteins have a closed range of 31.0% to 34.2% of carbon atoms irrespective of their origin and amino acid sequence. Further the protein interaction and functional enrichment analysis of AQP7 showed significant interaction with glycerol kinase and ATP-sensitive inward rectifier potassium channel protein. Our insilico analysis on aquaporin proteins exposed that nature tends to maintain the overall carbon atom composition in the proteins regardless of their amino acid sequence composition which could be further used for their classification. Also, the most highly interacting partners for AQPs are the potassium buffering channel proteins.
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