To study the structural unfolding of a globular protein with aromatic amino acids and multiple disulfide bonds as a function of pH, which of the following techniques would be the most appropriate?
1
Recording fluorescence emission spectra of tryptophan residues at varying pH
2
Monitoring the UV absorbance at 280 nm across different pH values
3
Estimating free sulfhydryl groups (-SH) content after treatment with a reducing agent
4
Measuring the circular dichroism spectra at varying pH
5
Question Not Attempted