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AFM structural study of the molecular chaperone GroEL and its two-dimensional crystals: an ideal "living" calibration sample.

作者信息

Valle F, DeRose J A, Dietler G, Kawe M, Plückthun A, Semenza G

机构信息

Institut de Physique de la Matière Condensèe, BSP, Université de Lausanne, Dorigny, Switzerland.

出版信息

Ultramicroscopy. 2002 Oct;93(1):83-9. doi: 10.1016/s0304-3991(02)00149-3.

DOI:10.1016/s0304-3991(02)00149-3
PMID:12380652
Abstract

Supramolecular complexes, such as chaperonins, are suitable samples for atomic force microscope structural studies because they have a very well defined shape. High-resolution images can be made using tapping mode in liquid under native conditions. Details about the two-dimensional structures formed onto the surface upon adsorption and of the single protein can be observed. Dissection of the upper ring of the supramolecular complex as a result of the applied lateral force through scanning tip is observed. Finally, the combination of lateral convolution and tip penetration into the cavity of chaperonins offers a direct evaluation of the tip convolution effect on images of macromolecular samples.

摘要

相似文献

1
AFM structural study of the molecular chaperone GroEL and its two-dimensional crystals: an ideal "living" calibration sample.
Ultramicroscopy. 2002 Oct;93(1):83-9. doi: 10.1016/s0304-3991(02)00149-3.
2
Chaperonins GroEL and GroES: views from atomic force microscopy.伴侣蛋白GroEL和GroES:原子力显微镜下的观察
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Single-molecule imaging by atomic force microscopy of the native chaperonin complex of the thermophilic archaeon Sulfolobus solfataricus.利用原子力显微镜对嗜热古菌嗜热栖热菌的天然伴侣蛋白复合物进行单分子成像。
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How to orient the functional GroEL-SR1 mutant for atomic force microscopy investigations.如何为原子力显微镜研究确定功能性GroEL-SR1突变体的方向。
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Imaging the native structure of the chaperone protein GroEL without fixation using atomic force microscopy.
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Atomic force microscopy applications in macromolecular crystallography.原子力显微镜在大分子晶体学中的应用。
Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1053-60. doi: 10.1107/s0907444901008824. Epub 2001 Jul 23.
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Protein folding assisted by the GroEL/GroES chaperonin system.由GroEL/GroES伴侣蛋白系统辅助的蛋白质折叠。
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Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL.快速扫描原子力显微镜揭示了GroEL的ATP/ADP依赖性构象变化。
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Atomic force microscopy and its related techniques in biomedicine.原子力显微镜及其在生物医学中的相关技术。
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Assessing the structure and function of single biomolecules with scanning transmission electron and atomic force microscopes.利用扫描透射电子显微镜和原子力显微镜评估单生物分子的结构和功能。
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