Specific mutations alter fibrillation kinetics, fiber morphologies, and membrane interactions of pentapeptides derived from human calcitonin.

Abstract excerpt

Protein misfolding and fibrillation are fundamental facets underlying a diverse group of amyloid disorders and diseases. The molecular factors responsible for amyloid protein toxicity and pathological consequences, however, are still not fully understood. The involvement of specific residues or sequence elements in fibril formation and the interactions of amyloid protein aggregates with membranes are believed to...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Calcitonin
• Share to Fluorescence Resonance Energy Transfer