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A model for non-obligate oligomer formation in protein aggregration.


ABSTRACT: 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).

SUBMITTER: Healy EF 

PROVIDER: S-EPMC4564312 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature

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A model for non-obligate oligomer formation in protein aggregration.

Healy Eamonn F EF  

Biochemical and biophysical research communications 20150815 3


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). ...[more]

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