[HTML][HTML] Intrinsic disorder and autonomous domain function in the multifunctional nuclear protein, MeCP2
VH Adams, SJ McBryant, PA Wade… - Journal of Biological …, 2007 - ASBMB
To probe the tertiary structure and domain organization of native methyl CpG-binding protein
2 (MeCP2), the recombinant human e2 isoform was purified to homogeneity and
characterized by analytical ultracentrifugation, CD, and protease digestion. The location of
intrinsic disorder in the MeCP2 sequence was predicted using the FoldIndex algorithm.
MeCP2 was found to be monomeric in low and high salt and over a nearly 1000-fold
concentration range. CD indicated that the MeCP2 monomer was nearly 60% unstructured …
2 (MeCP2), the recombinant human e2 isoform was purified to homogeneity and
characterized by analytical ultracentrifugation, CD, and protease digestion. The location of
intrinsic disorder in the MeCP2 sequence was predicted using the FoldIndex algorithm.
MeCP2 was found to be monomeric in low and high salt and over a nearly 1000-fold
concentration range. CD indicated that the MeCP2 monomer was nearly 60% unstructured …