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通过原子力显微镜在分子分辨率下对缓冲液中固定化蛋白质进行成像。

Immobilized proteins in buffer imaged at molecular resolution by atomic force microscopy.

作者信息

Weisenhorn A L, Drake B, Prater C B, Gould S A, Hansma P K, Ohnesorge F, Egger M, Heyn S P, Gaub H E

机构信息

Department of Physics, University of California, Santa Barbara 93106.

出版信息

Biophys J. 1990 Nov;58(5):1251-8. doi: 10.1016/S0006-3495(90)82465-6.

Abstract

Samples of supported planar lipid-protein membranes and actin filaments on mica were imaged by atomic force microscopy (AFM). The samples were fully submerged in buffer at room temperature during imaging. Individual proteins bound to the reconstituted membrane were distinguishable; some structural details could be resolved. Also, surface-induced, self-assembling of actin filaments on mica could be observed. Monomeric subunits were imaged on individual actin filaments. The filaments could be manipulated on or removed from the surface by the tip of the AFM. The process of the decoupling of the filamentous network from the surface upon changing the ionic conditions was imaged in real time.

摘要

通过原子力显微镜(AFM)对云母上负载的平面脂质 - 蛋白质膜和肌动蛋白丝样品进行成像。在成像过程中,样品完全浸没在室温下的缓冲液中。与重构膜结合的单个蛋白质是可区分的;一些结构细节可以分辨出来。此外,还可以观察到云母表面诱导的肌动蛋白丝自组装。在单个肌动蛋白丝上对单体亚基进行了成像。肌动蛋白丝可以通过AFM的尖端在表面上进行操作或从表面移除。实时成像了在改变离子条件时丝状网络与表面解耦的过程。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0245/1281069/da95fbf448a1/biophysj00121-0170-a.jpg

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