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

页码：6114 / 6117

页数：4

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