The lipocalins are a functionally diverse and divergent superfamily of proteins that share a common three dimensional structure which consists of an antiparallel �-barrel and a C-terminal a-helix. Lipocalins are found in various organisms with a wide range of functions such as pheromone activity, lipid transport and coloration. Even though lipocalins are found widely in nature, the first indication of its existence in plants was observed in late 20th century by the sequence analysis of Violaxanthin de-epoxidase and Zeaxanthin epoxidase, which were shown to be lipocalin-like proteins. Recently lipocalins from Wheat and Arabidopsis were identified as true lipocalins through the elucidation of three structurally conserved regions. The study of these lipocalins is vital as these proteins are believed to help plants tolerate oxidative stress and extreme conditions which broadens our understanding of plant sustainability in different environments.  We will present a detailed bioinformatics and network analysis of the lipocalin superfamily which furthers our understanding of the key determinants of structure, stability and folding.  These studies also shed insight into the structure, function and evolutionary relationships of the Triticum aestivum temperature induced lipocalin (Tatil) and reveals the first experimental characterization of stability and folding for this protein.

Key determinants of lipocalin protein evolution, stability, and folding

246th National Meeting (2013)

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