Thermodynamic Stability of a κI Immunoglobulin Light Chain: Relevance to Multiple Myeloma

Immunoglobulin light chains have two similar domains, each with a hydrophobic core surrounded by β-sheet layers, and a highly conserved disulfide bond. Differential scanning calorimetry and circular dichroism were used to study the folding and stability of MM- κI, an Ig LC of κI subtype purified fro...

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Veröffentlicht in:Biophysical journal 2005-06, Vol.88 (6), p.4232-4242
Hauptverfasser: Chung, Connie M., Chiu, Jenny D., Connors, Lawreen H., Gursky, Olga, Lim, Amareth, Dykstra, Andrew B., Liepnieks, Juris, Benson, Merrill D., Costello, Catherine E., Skinner, Martha, Walsh, Mary T.
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