Ontology highlight
ABSTRACT:
SUBMITTER: Morimoto D
PROVIDER: S-EPMC4309437 | biostudies-literature | 2015 Jan
REPOSITORIES: biostudies-literature
Morimoto Daichi D Walinda Erik E Fukada Harumi H Sou Yu-Shin YS Kageyama Shun S Hoshino Masaru M Fujii Takashi T Tsuchiya Hikaru H Saeki Yasushi Y Arita Kyohei K Ariyoshi Mariko M Tochio Hidehito H Iwai Kazuhiro K Namba Keiichi K Komatsu Masaaki M Tanaka Keiji K Shirakawa Masahiro M
Nature communications 20150120
Ubiquitin is known to be one of the most soluble and stably folded intracellular proteins, but it is often found in inclusion bodies associated with various diseases including neurodegenerative disorders and cancer. To gain insight into this contradictory behaviour, we have examined the physicochemical properties of ubiquitin and its polymeric chains that lead to aggregate formation. We find that the folding stability of ubiquitin chains unexpectedly decreases with increasing chain length, resul ...[more]