@article{open2182,
          volume = {165},
          number = {2},
           month = {February},
          author = {Rishu Jain and Deepak Sharma and Rakesh Kumar and Rajesh Kumar},
            note = {Copyright of this article belongs to OUP.},
           title = {Structural, kinetic and thermodynamic characterizations of SDS-induced molten globule state of a highly negatively charged cytochrome c.},
       publisher = {Oxford University Press },
            year = {2019},
         journal = {Journal of biochemistry},
           pages = {125--137},
        keywords = {alkali molten-globule, constrained dynamics, entropic stabilization, SDS, thermal stability},
             url = {http://crdd.osdd.net/open/2182/},
        abstract = {This study presents the structural, kinetic and thermodynamic characterizations of previously unknown submicellar concentrations of SDS-induced molten globule (MGSDS) state of a highly negatively charged base-denatured ferricytochrome c (UB-state) at pH {$\sim$}12.8 ({$\pm$}0.2). The far-UV CD, near-UV CD, ANS-fluorescence data of UB-state in the presence of different concentrations of SDS indicate that the submicellar concentrations of SDS ({$\leq$}0.4 mM) transform the UB-state to MGSDS-state. The MGSDS-state has native-like {\ensuremath{\alpha}}-helical secondary structure but lacks tertiary structure. The free energy change ({\ensuremath{\Delta}}G?D) for UB{$\rightarrow$} MGSDS transition determined by far-UV CD ({$\sim$}2.7 kcal mol-1) is slightly higher than those determined by fluorescence ({$\sim$}2.0 kcal mol-1) at 25?C. At very low SDS and NaCl concentrations, the MGSDS-state undergoes cold denaturation. As SDS concentration is increased, the thermal denaturation temperature increases and the cold denaturation temperature decrease. Kinetic experiments involving the measurement of the CO-association rate to the base-denatured ferrocytochrome c at pH {$\approx$}12.8 ({$\pm$}0.2), 25?C indicate that the submicellar concentrations of SDS restrict the internal dynamics of base-denatured protein.}
}