Resonance Raman and fluorescence spectroscopy are complementary techniques that elucidate molecular structures, microenvironments, and dynamics of biomolecules. We have applied these tools to investigate the folding mechanisms of an integral membrane protein, OmpA. The vibrational results highlight changes in structure and microenvironment of stabilizing tryptophan residues upon insertion and folding into lipid bilayers. Fluorescence data complement the vibrational data, and reveal evolution of global structure and changes in solvent accessibility. Collectively, both techniques reveal the timescales associated with various events during a folding reaction. These findings augment the previously proposed mechanisms for OmpA folding, and reveal the range of molecular detail that can be obtained with these techniques.

Resonance Raman and fluorescence investigations of membrane protein folding

251st National Meeting (2016)

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