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 from...

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Autores principales: 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.
Formato: Artigo
Lenguaje:Inglês
Publicado: Biophysical Society 2005
Materias:
Proteins
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC1305653/
https://ncbi.nlm.nih.gov/pubmed/15792972
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1529/biophysj.105.061317
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