Format

Send to

Choose Destination
See comment in PubMed Commons below
Amyloid. 2007 Jun;14(2):119-31.

Aggregation drives "misfolding" in protein amyloid fiber formation.

Author information

  • 1Biological Sciences Department, Florida Institute of Technology, Melbourne, FL 32901, USA. xshaohua@fit.edu

Abstract

Protein amyloid fibers are often found to have a beta-pleated sheet structure regardless of their sequence, leading some to believe that it is the molecule's misfolding that leads to aggregation. In this article, an alternative model is introduced for the amyloid community to consider, that fiber formation is a surface-energy minimization process, starting with the generation of colloidal particles and their linear assembly, and ending with structural evolution of the aggregates into mature fibers. We propose that aggregation drives conformational change and that a conformational change is not essential to initiate the aggregation process.

[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Taylor & Francis
    Loading ...
    Write to the Help Desk