Oligomeric states along the folding pathways of β2-microglobulin: kinetics, thermodynamics, and structure.

@article{Rennella2013OligomericSA,
  title={Oligomeric states along the folding pathways of β2-microglobulin: kinetics, thermodynamics, and structure.},
  author={Enrico Rennella and Thomas Cutuil and Paul Schanda and Isabel S{\'a}nchez Ayala and Frank Gabel and Vincent Forge and Alessandra Corazza and Gennaro Esposito and Bernhard Brutscher},
  journal={Journal of molecular biology},
  year={2013},
  volume={425 15},
  pages={
          2722-36
        }
}
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 fibril formation. Here, we investigated the… CONTINUE READING
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