title: Difference in fibril core stability between two tau four-repeat domain proteins: a hydrogen-deuterium exchange coupled to mass spectrometry study.
abstract: One of the signatures of Alzheimer's disease and tauopathies is fibrillization of the microtubule-associated protein tau. The purpose of this study was to compare the high-resolution structure of fibrils formed by two different tau four-repeat domain constructs, tau4RD and tauK18, using hydrogen-deuterium exchange coupled to mass spectrometry as a tool. While the two fibrils are found to be constructed on similar structural principles, the tauK18 fibril has a slightly more stable core. This difference in fibril core stability appears to be reflective of the mechanistic differences in the aggregation pathways of the two proteins.
authors.affiliation: National Centre for Biological Sciences, Tata Institute of Fundamental Research , Bangalore 560 065, India.
authors.forename: Gayathri
authors.initials: G
authors.lastname: Ramachandran
authors.forename: Jayant B
authors.initials: JB
authors.lastname: Udgaonkar
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism; D020816:Amino Acid Motifs; D041961:Deuterium Exchange Measurement; D006801:Humans; D013058:Mass Spectrometry; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D055550:Protein Stability; D020836:Protein Structure, Quaternary; D016875:tau Proteins / Q000737:chemistry*
chemical_list: D016875:tau Proteins