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纳米技术与蛋白质力学

Nanotechnology and protein mechanics.

作者信息

Ikai A, Idiris A, Wang T, Alam M T, Afrin R, Hyonchol K, Sekiguchi H, Nishida S, Arakawa H, Osada T

机构信息

Laboratory of Biodynamics, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta Midoriku, Yokohama, 226-8501 Japan.

出版信息

J Biol Phys. 2002 Dec;28(4):561-72. doi: 10.1023/A:1021252017832.

DOI:10.1023/A:1021252017832
PMID:23345798
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3456472/
Abstract

The atomic force microscope is currently used in our and many other laboratories to measure the mechanical response of polypeptide and proteins against tensile forces applied to well defined positions in their chemical structures. The resulting force vs. extension (F-E) curves are analyzed in relation to their known conformations under various conditions. The method can be extended to study the mechanical responses of other, often much larger biological structures, and extract the component proteins and DNAs from cell membranes and chromosomes.

摘要

目前,我们实验室和许多其他实验室都在使用原子力显微镜来测量多肽和蛋白质在其化学结构中特定位置所受拉力时的力学响应。根据所得的力与伸长(F-E)曲线,分析它们在各种条件下的已知构象。该方法可扩展用于研究其他通常大得多的生物结构的力学响应,并从细胞膜和染色体中提取组成蛋白和DNA。

相似文献

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Nanotechnology and protein mechanics.纳米技术与蛋白质力学
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2
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本文引用的文献

1
Specific interaction between GroEL and denatured protein measured by compression-free force spectroscopy.通过无压缩力谱法测量GroEL与变性蛋白之间的特异性相互作用。
Biophys J. 2003 Jul;85(1):484-90. doi: 10.1016/S0006-3495(03)74493-2.
2
Unfolding mechanics of holo- and apocalmodulin studied by the atomic force microscope.通过原子力显微镜研究全钙调蛋白和脱辅基钙调蛋白的展开机制。
Protein Sci. 2002 Jun;11(6):1532-8. doi: 10.1110/ps.3600102.
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Force measurement and inhibitor binding assay of monomer and engineered dimer of bovine carbonic anhydrase B.
Biochem Biophys Res Commun. 2001 Jul 6;285(1):9-14. doi: 10.1006/bbrc.2001.5118.
4
Differences in zero-force and force-driven kinetics of ligand dissociation from beta-galactoside-specific proteins (plant and animal lectins, immunoglobulin G) monitored by plasmon resonance and dynamic single molecule force microscopy.通过表面等离子体共振和动态单分子力显微镜监测的β-半乳糖苷特异性蛋白质(植物和动物凝集素、免疫球蛋白G)配体解离的零力和力驱动动力学差异。
Arch Biochem Biophys. 2000 Nov 15;383(2):157-70. doi: 10.1006/abbi.2000.1993.
5
Spring mechanics of alpha-helical polypeptide.α-螺旋多肽的弹簧力学
Protein Eng. 2000 Nov;13(11):763-70. doi: 10.1093/protein/13.11.763.
6
How strong is a covalent bond?共价键的强度如何?
Science. 1999 Mar 12;283(5408):1727-30. doi: 10.1126/science.283.5408.1727.
7
The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy.通过原子力显微镜测量肌蛋白肌联蛋白中免疫球蛋白和纤连蛋白III结构域的机械稳定性。
Biophys J. 1998 Dec;75(6):3008-14. doi: 10.1016/S0006-3495(98)77741-0.
8
Retrieval and amplification of single-copy genomic DNA from a nanometer region of chromosomes: a new and potential application of atomic force microscopy in genomic research.从染色体纳米区域检索和扩增单拷贝基因组DNA:原子力显微镜在基因组研究中的一种新的潜在应用。
Biochem Biophys Res Commun. 1998 Jul 30;248(3):744-8. doi: 10.1006/bbrc.1998.9027.
9
Specific antigen/antibody interactions measured by force microscopy.通过力显微镜测量的特异性抗原/抗体相互作用。
Biophys J. 1996 May;70(5):2437-41. doi: 10.1016/S0006-3495(96)79814-4.
10
Detection and localization of individual antibody-antigen recognition events by atomic force microscopy.通过原子力显微镜检测和定位单个抗体 - 抗原识别事件。
Proc Natl Acad Sci U S A. 1996 Apr 16;93(8):3477-81. doi: 10.1073/pnas.93.8.3477.