Nano-Chemical Infrared Imaging of Membrane Proteins in Lipid Bilayers

被引:101
作者
Berweger, Samuel [1 ,2 ,5 ,6 ]
Nguyen, Duc M. [3 ]
Muller, Eric A. [1 ,2 ,5 ,6 ]
Bechtel, Hans A. [7 ]
Perkins, Thomas T. [4 ,5 ,6 ]
Raschke, Markus B. [1 ,2 ,5 ,6 ]
机构
[1] Univ Colorado, Dept Phys, Boulder, CO 80309 USA
[2] Univ Colorado, Dept Chem, Boulder, CO 80309 USA
[3] Univ Colorado, Dept Chem & Biol Engn, Boulder, CO 80309 USA
[4] Univ Colorado, Dept Mol Cellular & Dev Biol, Boulder, CO 80309 USA
[5] Univ Colorado, NIST, Joint Inst Lab Astrophys, Boulder, CO 80309 USA
[6] Univ Colorado, Boulder, CO 80309 USA
[7] Univ Calif Berkeley, Lawrence Berkeley Natl Lab, Adv Light Source Div, Berkeley, CA 94720 USA
基金
美国国家科学基金会;
关键词
ATOMIC-FORCE MICROSCOPY; NEAR-FIELD MICROSCOPY; OPTICAL MICROSCOPY; PURPLE MEMBRANES; SPECTROSCOPY; RESOLUTION; BACTERIORHODOPSIN; LIMIT; SCATTERING; STABILITY;
D O I
10.1021/ja409815g
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The spectroscopic characterization of biomolecular structures requires nanometer spatial resolution and chemical specificity. We perform full spatio-spectral imaging of dried purple membrane patches purified from Halobacterium salinarum with infrared vibrational scattering-type scanning near-field optical microscopy (s-SNOM). Using near-field spectral phase contrast based on the Amide I resonance of the protein backbone, we identify the protein distribution with 20 nm spatial resolution and few-protein sensitivity. This demonstrates the general applicability of s-SNOM vibrational nanospectroscopy, with potential extension to a wide range of biomolecular systems.
引用
收藏
页码:18292 / 18295
页数:4
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