Healy Eamonn F
Department of Chemistry, St. Edward's University, Austin, TX 78704, USA.
Biochem Biophys Res Commun. 2015 Sep 25;465(3):523-7. doi: 10.1016/j.bbrc.2015.08.052. Epub 2015 Aug 15.
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).
利用溶剂暴露的分子内主链氢键作为蛋白质堆积的物理化学描述符,提出了瞬时、非必需寡聚体在异常蛋白质聚集体形成中的作用。提出了超氧化物歧化酶(SOD1)野生型(wt)和选定突变变体的寡聚体模型,为研究肌萎缩侧索硬化症(ALS)的病因提供结构基础。