Oligomeric States along the Folding Pathways of β2-Microglobulin: Kinetics, Thermodynamics, and Structure

Volume: 425, Issue: 15, Pages: 2722 - 2736
Published: Aug 1, 2013
Abstract
The transition of proteins from their soluble functional state to amyloid fibrils and aggregates is associated with the onset of several human diseases. Protein aggregation often requires some structural reshaping and the subsequent formation of intermolecular contacts. Therefore, the study of the conformation of excited protein states and their ability to form oligomers is of primary importance for understanding the molecular basis of amyloid...
Paper Details
Title
Oligomeric States along the Folding Pathways of β2-Microglobulin: Kinetics, Thermodynamics, and Structure
Published Date
Aug 1, 2013
Volume
425
Issue
15
Pages
2722 - 2736
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