Abstract
In this work, we have analyzed the influence of ?-? interactions on stability and properties of Sm/LSm assemblies. Phe residues were found to be involved in ?-? interactions much more frequently than Tyr or His. Similarly, the Phe-Phe ?-? interacting pair had the highest frequency of occurrence. Furthermore, a significant number of ?-networks were observed at the interface of Sm/LSm proteins. Generally speaking, the distance between the interacting pairs was in the range of 5-6 ?. 3? and 7?-networks were found to frequently have plane-plane angles less than 60?. Solvent accessibility pattern of Sm/LSm proteins revealed that all of the interacting residues were from buried areas. Moreover, most of the ?-? interacting residues of Sm/LSm proteins were evolutionary conserved and were in the strand regions. A high percentage of these residues could be considered as stabilization centers that (significantly) contribute to the net stability of Sm/LSm proteins.
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