Journal
NATURE STRUCTURAL BIOLOGY
Volume 9, Issue 5, Pages 326-331Publisher
NATURE AMERICA INC
DOI: 10.1038/nsb791
Keywords
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Funding
- Biotechnology and Biological Sciences Research Council [SF16972] Funding Source: Medline
- Biotechnology and Biological Sciences Research Council [SF16972] Funding Source: researchfish
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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 H-1-N-15 NMR to determine the conformational properties of an amyloidogenic intermediate of human beta(2)-microglobulin (beta(2)m) 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 beta-strands that comprise the native fold. The amyloid precursors of beta(2)m 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.
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