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.
biochemistry, biothermics, molecular biophysics, molecular configurations, proteins
Biochemistry | Biophysics | Molecular Biology
© 2011 American Institute of Physics
American Institute of Physics
Park, Byoung Kyoo; Yi, Namwoo; Park, Jaesung; Choi, Tae Y.; Lee, Jin Young; Busnaina, Ahmed; and Kim, Dongsik, "Thermal conductivity of bovine serum albumin: a tool to probe denaturation of protein" (2011). Mechanical and Industrial Engineering Faculty Publications. Paper 38. http://hdl.handle.net/2047/d20001186
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