Browse by author
Lookup NU author(s): Professor Steve Homans
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
The population of one or more partially folded states has been proposed as a critical initial step in amyloid formation for several proteins. Here we use equilibrium denaturation measured by 1H-15N NMR to determine the conformational properties of an amyloidogenic intermediate of human 2-microglobulin (2m) formed at low pH. The data show that this amyloid precursor is a noncooperatively stabilized ensemble that retains stable structure in five of the seven -strands that comprise the native fold. The amyloid precursors of 2m and transthyretin have similar properties despite having structurally unrelated native folds. The data offer a rationale as to why these proteins are both amyloidogenic at low pH and suggest that amyloidosis of these and other proteins may involve ordered assembly from a precursor with similar conformational features.
Author(s): McParland VJ, Kalverda AP, Homans SW, Radford SE
Publication type: Article
Publication status: Published
Journal: Nature Structural Biology
Year: 2002
Volume: 9
Pages: 326-331
ISSN (print): 1545-9993
ISSN (electronic): 1545-9985
Publisher: Nature Publishing Group
URL: http://dx.doi.org/10.1038/nsb791
DOI: 10.1038/nsb791
Altmetrics provided by Altmetric