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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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| Autors principals: | , , , , , , , , , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
Biophysical Society
2005
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| Matèries: | |
| Accés en línia: | 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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