Abstract
Dehydrin is an IDP that belongs to the Late Embryogenesis Abundant protein family which has been shown to have important role in abiotic stress tolerance. Here, we investigated the DHN1 (dehydrin) protein from Zea mays (167 aa). The role of conserved segment and its folding in presence of membrane is vital for understanding the functional mechanism of DHN1. To investigate the structural change and cryoprotection mechanism of DHN1, three mutants: DHN1 CW1 (Trp122–Cys62), DHN1 CW2 (Trp132–Cys62) and DHN1 W3 (Trp3) were generated using site directed mutagenesis.
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