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]]). 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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Many [[X-ray crystallography|crystallographic]] structures have missing loops -- that is, ranges of amino acids with no [[atomic coordinate file|atomic coordinates]] in the model. These "gaps" in the model are often thought to be artifacts of inadvertant disorder in the crystal. In some cases, these gaps may be alerting us to the presence of intrinsically disordered loops in an otherwise folded protein<ref name="IDSG" />. Such gaps are the basis for the [[#Protein disorder predictors|DISOPRED2 disorder prediction server]]. [[FirstGlance in Jmol]] offers [[Temperature_value#Missing_Residues|one method for locating and visualizaing such gaps]]. | Many [[X-ray crystallography|crystallographic]] structures have missing loops -- that is, ranges of amino acids with no [[atomic coordinate file|atomic coordinates]] in the model. These "gaps" in the model are often thought to be artifacts of inadvertant disorder in the crystal. In some cases, these gaps may be alerting us to the presence of intrinsically disordered loops in an otherwise folded protein<ref name="IDSG" />. Such gaps are the basis for the [[#Protein disorder predictors|DISOPRED2 disorder prediction server]]. [[FirstGlance in Jmol]] offers [[Temperature_value#Missing_Residues|one method for locating and visualizaing such gaps]]. | ||
