Structural characterization of the partially folded intermediates of an immunoglobulin light chain leading to amyloid fibrillation and amorphous aggregation.

@article{Qin2007StructuralCO,
  title={Structural characterization of the partially folded intermediates of an immunoglobulin light chain leading to amyloid fibrillation and amorphous aggregation.},
  author={Zhijie Qin and Dongmei Hu and Min hao Zhu and Anthony L. Fink},
  journal={Biochemistry},
  year={2007},
  volume={46 11},
  pages={
          3521-31
        }
}
Immunoglobulin light chain deposition diseases involve various types of extracellular deposition of light chain variable domains, including amyloid fibrils and amorphous deposits. The decreased thermodynamic stability of the light chain is believed to be the major factor leading to fibrillation. However, the differences in the nature of the deposits among the light chain deposition diseases raise the question of whether the mechanisms leading to fibrillar or amorphous aggregation is different… CONTINUE READING
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