An Exploration of the Universe of Polyglutamine Structures.

ABSTRACT: Deposits of misfolded proteins in the human brain are associated with the development of many neurodegenerative diseases. Recent studies show that these proteins have common traits even at the monomer level. Among them, a polyglutamine region that is present in huntingtin is known to exhibit a correlation between the length of the chain and the severity as well as the earliness of the onset of Huntington disease. Here, we apply bias exchange molecular dynamics to generate structures of polyglutamine expansions of several lengths and characterize the resulting independent conformations. We compare the properties of these conformations to those of the standard proteins, as well as to other homopolymeric tracts. We find that, similar to the previously studied polyvaline chains, the set of pos

SUBMITTER: Gomez-Sicilia A 

PROVIDER: S-EPMC4619799 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature