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.
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
Permanent URL
Recommended Citation
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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Biochemistry Commons, Biophysics Commons, Molecular Biology Commons
Notes
Originally published in Applied Physics Letters, v.99, 163702 (2011). doi:10.1063/1.3652704