چكيده لاتين :
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 (DHcal) to van’t Hoff enthalpy (DHVH), 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 H1 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.
