期刊
JOURNAL OF THE IRANIAN CHEMICAL SOCIETY
卷 2, 期 3, 页码 189-196出版社
SPRINGER
DOI: 10.1007/BF03245921
关键词
SDS; proteins; enthalpy; molten globule; folding; unfolding
The anionic surfactant sodium n-dodecyl sulfate (SDS) plays a variety of roles with regard to protein conformation, depending on its concentration. SDS at low concentrations mostly induces the compaction of protein (folding). Examples of this include: the molten globule state of acid-unfolded cytochrome c, associated with enhancement of the exothermic enthalpy values of isothermal titration calorimetry and a reversible profile by differential scanning calorimetry; the enzyme activation and compaction of Aspergillus niger catalase, and relationship of calorimetric enthalpy (Delta H-cal) to van't Hoff enthalpy (Delta H-VH), which proves the existence of intermolecular and intramolecular interaction during enzyme activation by SDS; the production of a new energetic domain for human apotransferrin and folded state for histone H-1 by SDS. SDS at moderate concentrations below the critical micelle concentration (cmc) is a potent denaturant for protein in solution. Protein denaturation is a key method in thermodynamics and binding site analysis and can be used to enhance our understanding of the protein structure-function relationship. The interaction between protein and surfactant, such as SDS, at the cmc level is a complicated interaction, thermodynamically, that should bring about enthalpy correction through micellar dissociation and micelle dilution.
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