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- W2013185434 abstract "The secondary structure of the retrovirus integration protein (IN) was predicted from seven inferred retrovirus IN sequences. The IN sequences were aligned by computer and the phylogenetic relationships between them were determined. The secondary structure of the aligned IN sequences was predicted by two consensus prediction methods. The predicted secondary structural patterns from the two consensus prediction schemes were compared with and superimposed on a composite structural profile of hydropathic/chain flexibility/amphipathic indexes with each index profile being calculated independently for the aligned IN sequences. The use of this composite structural profile not only enhanced the prediction accuracy but also helped in defining the surface loop regions which would be otherwise unpredictable by the use of consensus prediction methods alone. An amphipathic helix was identified by these united structural prediction-chain property profiles. Helical wheel analysis gave the amphipathic helix a coiled-coil like pattern which was similar to the leucine zipper discovered for some eukaryotic gene regulatory proteins. The proposed amphipathic helix may play an essential role in defining the biological properties of IN." @default.
- W2013185434 created "2016-06-24" @default.
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- W2013185434 date "1991-01-01" @default.
- W2013185434 modified "2023-09-27" @default.
- W2013185434 title "Retrovirus integrase: identification of a potential leucine zipper motif" @default.
- W2013185434 doi "https://doi.org/10.1093/protein/4.4.435" @default.
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