Intrinsically Disordered Protein: Difference between revisions
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At left is an animation of a heat shock/chaperonin protein fragment. Residues 1-70 are disordered; 71-109 are alpha helical. This animates 20 models from an NMR experiment ([[2ljl]]). For comparison, at right is an animation of 20 NMR models of a protein of similar length that folds into a stable domain ([[2n5a]]). | At left is an animation of a heat shock/chaperonin protein fragment. Residues 1-70 are disordered; 71-109 are alpha helical. This animates 20 models from an NMR experiment ([[2ljl]]). Charges are colored <font color="blue">'''blue=positive'''</font> and <font color="red">'''red=negative'''</font>. A high charge density prevents folding. For comparison, at right is an animation of 20 NMR models of a protein of similar length that folds into a stable domain ([[2n5a]]). | ||
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Animations will stop after 25 cycles. Re-load this page to restart the animations. | |||
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