| Literature DB >> 9600926 |
J le Coutre1, H R Kaback, C K Patel, L Heginbotham, C Miller.
Abstract
The structure of the tetrameric K+ channel from Streptomyces lividans in a lipid bilayer environment was studied by polarized attenuated total reflection Fourier transform infrared spectroscopy. The channel displays approximately 43% alpha-helical and 25% beta-sheet content. In addition, H/D exchange experiments show that only 43% of the backbone amide protons are exchangeable with solvent. On average, the alpha-helices are tilted 33 degrees normal to the membrane surface. The results are discussed in relationship to the lactose permease of Escherichia coli, a membrane transport protein.Entities:
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Year: 1998 PMID: 9600926 PMCID: PMC27594 DOI: 10.1073/pnas.95.11.6114
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205