Abstract

We demonstrate a strong correlation between denaturation of bovine serum albumin (BSA) and the thermal conductivity k of aqueous solutions of BSA. When denaturation of BSA began, k dropped significantly. These results suggest that k, i.e., the ability of a protein to transport passively applied thermal energy, can be exploited to probe the conformational dynamics of BSA and potentially of other proteins. The technique of protein analysis demonstrated in this work is expected to be useful in micro-total-analysis systems because it is easier to miniaturize and to integrate into a device than is conventional differential scanning calorimetry analysis.

Notes

Originally published in Applied Physics Letters, v.99, 163702 (2011). doi:10.1063/1.3652704

Keywords

biochemistry, biothermics, molecular biophysics, molecular configurations, proteins

Disciplines

Biochemistry | Biophysics | Molecular Biology

Publication Date

10-19-2011

Rights Information

© 2011 American Institute of Physics

Rights Holder

American Institute of Physics

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