eight histones assembled together in a nucleosome is an example of a protein’s folding.
eight histones assembled together in a nucleosome is an example of a protein’s?
folding
Na
Na
unlike the other histones, h1 does not make up the nucleosome "bead". instead, it sits on top of the structure, keeping in place the dna that has wrapped around the nucleosome. h1 is present in half the amount of the other four histones, which contribute two molecules to each nucleosome bead. in addition to binding to the nucleosome, the h1 protein binds to the "linker dna" (approximately 20-80 nucleotides in length) region between nucleosomes, helping stabilize the zig-zagged 30 nm chromatin fiber. much has been learned about histone h1 from studies on purified chromatin fibers. ionic extraction of linker histones from native or reconstituted chromatin promotes its unfolding under hypotonic conditions from fibers of 30 nm width to beads-on-a-string nucleosome arrays.
histone h1