title: A glimpse of a possible amyloidogenic intermediate of transthyretin.
abstract: Studies have indicated that partially unfolded states occur under conditions that favor amyloid formation by transthyretin (TTR), as well as other amyloidogenic proteins. In this study, we used hydrogen exchange measurements to show that there is selective destabilization of one half of the beta-sandwich structure of TTR under such conditions. This provides more direct information about conformational fluctuations than previously available, and will facilitate design of future experiments to probe the intermediates critical to amyloid formation.
authors.affiliation: Department of Chemistry, MC-1460, Lawrence Berkeley National Laboratory, University of California, Berkeley, CA 94720-1460, USA.
authors.forename: K
authors.initials: K
authors.lastname: Liu
authors.forename: H S
authors.initials: HS
authors.lastname: Cho
authors.forename: H A
authors.initials: HA
authors.lastname: Lashuel
authors.forename: J W
authors.initials: JW
authors.lastname: Kelly
authors.forename: D E
authors.initials: DE
authors.lastname: Wemmer
mesh_terms: D000577:Amides / Q000378:metabolism; D003903:Deuterium / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D058225:Plaque, Amyloid / Q000737:chemistry* / Q000378:metabolism*; D011228:Prealbumin / Q000737:chemistry* / Q000378:metabolism*; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D011522:Protons
chemical_list: D000577:Amides; D011228:Prealbumin; D011522:Protons; D003903:Deuterium