Abstract: Disordered Proteins are active proteins, some part of which may not have a specific three-dimensional structure. They are known to adopt a specific structure in conjunction with its binding partner. They lack hydrophobic amino acids that help in the process of protein folding. Late Embryogenesis Abundant proteins help in protecting higher plants from damages caused by environmental stresses. We analyzed randomly selected LEA proteins and transcription factors of plants and animals for various parameters of disorderness and compared them with proteins of Arabidopsis thaliana and Caenorhabditis elegans. The disordered percentage in each of these proteins was calculated using PONDR. Their amino acid composition, hydropathicity values were obtained by Protparam. The Ramachandran plot was used to obtain favorable and unfavorable regions. Some of the structures which were not available in structural databases were modeled using Alpha Fold 2. Our results show that the disordered percentages in LEA proteins transcription factors are statistically higher compared to normal proteins in Arabidopsis thaliana and Caenorabhditis elegans. We speculate that the necessity of LEA proteins to function in stressful developmental conditions and the necessity of the transcription factors to bind to multiple partners ( both DNA elements and other factors) may be the reason why these groups of proteins exhibit such high percentages of disorderness.

Keywords: Disordered proteins, Late Embryogenesis Abundant protein, Transcription factor, Hydropathicity, Alpha fold 2.

| DOI: 10.17148/IARJSET.2022.9271