A model for non-obligate oligomer formation in protein aggregration.
Using solvent-exposed intramolecular backbone hydrogen bonds as physico-chemical descriptors for protein packing, a role for transient, non-obligate oligomers in the formation of aberrant protein aggregates is presented. Oligomeric models of the both wild type (wt) and select mutant variants of superoxide dismutase (SOD1) are proposed to provide a structural basis for investigating the etiology of Amyotrophic Lateral Sclerosis (ALS).
Department of Chemistry, St. Edward's University, Austin, TX 78704, USA. Electronic address: healy@stedwards.edu.
Eamonn F
EF
Healy
D001665:Binding Sites; D006860:Hydrogen Bonding; D008956:Models, Chemical; D062105:Molecular Docking Simulation; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000648:ultrastructure*; D011485:Protein Binding; D011487:Protein Conformation; D013482:Superoxide Dismutase / Q000737:chemistry* / Q000648:ultrastructure*; D000072105:Superoxide Dismutase-1
D046912:Multiprotein Complexes; D013482:Superoxide Dismutase; D000072105:Superoxide Dismutase-1
Dehydron; Obligate non-obligate oligomer; SOD1