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Structural properties of an amyloid precursor ofβ2-microglobulin

Lookup NU author(s): Professor Steve Homans


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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.

Publication metadata

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


DOI: 10.1038/nsb791


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