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

被引：76
|
作者：
le Coutre, J
Kaback, HR
Patel, CKN
Heginbotham, L
Miller, C
机构：
[1] Univ Calif Los Angeles, Howard Hughes Med Inst, MacDonald Res Labs 6 720, Dept Physiol, Los Angeles, CA 90095 USA
[2] Univ Calif Los Angeles, Inst Mol Biol, Dept Microbiol & Mol Genet, Los Angeles, CA 90095 USA
[3] Univ Calif Los Angeles, Dept Phys & Astron, Los Angeles, CA 90095 USA
[4] Brandeis Univ, Howard Hughes Med Inst, Dept Biochem, Waltham, MA 02254 USA
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1998年 / 95卷 / 11期
关键词：
D O I：
10.1073/pnas.95.11.6114
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
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.
引用
收藏
页码：6114 / 6117
页数：4
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