Deep UV resonance Raman spectral properties of alpha helical membrane proteins
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Membrane protein function and structure determination is vital for pharmaceutical development and disease prevention. Despite the various methods of protein structure elucidation in use, a need still exists for techniques that are of adequate resolution, rapid, inexpensive, and compatible with the membrane environment of these proteins. Deep UV resonance Raman (dUVRR) spectroscopy is an emerging structurally sensitive spectroscopic technique for analyzing membrane protein structure. The backbone amide modes are resonance enhanced in dUVRR spectra while the membrane's lipid features are not, resulting in strong membrane protein spectral features in near native environments. In order to better define dUVRR spectral features of membrane proteins, a series of model helical peptides, poly(LA)7, were designed. By substituting select residues of the transmembrane region of poly(LA)7, the propensity of helical structure within a membrane has also been studied. Using these model membrane peptides in increasingly dehydrated environments (aqueous, surfactant, and bilayer), hydration depended changes in the spectra are characterized.
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