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The structure of the tetrameric K+ channel fromStreptomyces lividans in a lipid bilayer environment was studied by polarized attenuated total reflection Fourier transform infrared spectroscopy. The channel displays approximately 43% α-helical and 25% β-sheet content. In addition, H/D exchange experiments show that only 43% of the backbone amide protons are exchangeable with solvent. On average, the α-helices are tilted 33° normal to the membrane surface. The results are discussed in relationship to the lactose permease ofEscherichia coli , a membrane transport protein.

Fourier transform infrared spectroscopy reveals a rigid α-helical assembly for the tetrameric Streptomyces lividans K + channel

Fourier transform infrared spectroscopy reveals a rigid α-helical assembly for the tetrameric Streptomyces lividans K ⁺ channel