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Fig. 5 | BMC Genomics

Fig. 5

From: An evolutionary roadmap to the microtubule-associated protein MAP Tau

Fig. 5

Display of exon structure, conservation and biophysical properties of MAPT on a potential structural model of human MAPTv6. Exon distribution (a) with red-boxed inset showing a MAPT fragment (602–647 in 776 aa isoform 6) that adopts a more stable helical structure when bound to tubulin [6], pbd:2MZ7; site-specific evolutionary conservation calculated by CONSURF (b); surface maps of hydrophobicity by CHIMERA (c); and surface electric potential from APBS (d) are shown. The predicted model with highest confidence score from I-Tasser was reconstructed by threading template fragments from the Protein Data Bank and ab initio modeling with consideration of steric constraints and low free-energy state. Note that MAPT is an intrinsically disordered protein without fixed constraints on 3D crystal or solution structure [18], so this model is intended mainly as a display platform for the protein physicochemical properties

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