Recent electrophysiology studies in our laboratory suggest that some proteins from the Serine Protease Inhibitor (SERPIN) family cross cell membranes without regulated uptake mechanisms. Since these proteins do not structurally resemble typical membrane proteins, questions arise about the factors governing interactions between lipid and protein of this family. Previous studies of ovalbumin_a chicken protein of the SERPIN family_indicate that both glycosylation and phosphorylation play vital regulatory roles. Combining UV-visible and phosphorus NMR spectroscopy offers information on these posttranslational modifications. Proteins crossing the cell membrane must enter the central region of lipid tails. This hydrophobic environment causes the proteins to change conformation and altering the absorbance and resonance spectra. In UV-spectroscopy, environmental hydrophobicity cause phenylalanine, tyrosine, and tryptophan peaks to shift. In P31 NMR, the hydrophobic interactions lead to changes in phosphorus chemical shifts. Combining information from both these methods reveals the interactions of phosphorylated glycoproteins and lipid bilayers.
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