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Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases
1Department of Chemistry, Texas A&M University, College Station, Texas, 77843-3255, USA. kelly@chemvx.tamu.edu
Structure (London, England : 1993)
|May 15, 1997
Abstract:
The assembly and misassembly of normally soluble proteins into fibrilar structures is thought to be a causative agent in a variety of human amyloid and prion diseases. Structural and mechanistic studies of this process are beginning to elucidate the conformational changes required for the conversion of a normally soluble and functional protein into a defined quaternary structure.
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