Title : Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase.

Pub. Date : 2007 Jun 12

PMID : 17548825






3 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 A growing body of evidence suggests that in familial ALS (FALS) it is the molecular behavior of the metal-depleted SOD1 dimer that leads to a gain of toxic properties by misfolding, unfolding, and aggregation. Metals superoxide dismutase 1 Homo sapiens
2 Here, using our 1.15-A resolution structure of fully metallated human SOD1 and highly parallelized molecular dynamics code on a high-performance capability computer, we have undertaken molecular dynamics calculations to 4,000 ps to reveal the first stages of misfolding caused by metal deletion. Metals superoxide dismutase 1 Homo sapiens
3 These calculations reveal an essential step in the formation of the experimentally observed self-aggregations of metal-depleted FALS mutant SOD1. Metals superoxide dismutase 1 Homo sapiens