Question

5. The hypothetical protein E contains no tyrosine residues and 3 tryptophan residues. When in the native folding state, protein E displays maximum emissions at 302 and 330 nm when excited using light at 280 nm. However, when denatured, the observed emission maximum shifts to 350 nm. Please explain briefly why two separate emissions maxima are observed in the native state (address intra- or inter-molecular interactions). Also, please briefly explain why such a shift in emissions occurs upon protein unfolding and describe the environment that likely surrounds each tryptophan residue in the native state.

Answer 1