Noninvasive Protein Structural Flexibility Mapping by Bimodal Dynamic Force Microscopy

被引：114

作者：

Martinez-Martin, D. ^{[1
]}

Herruzo, E. T. ^{[2
]}

Dietz, C. ^{[2
]}

Gomez-Herrero, J. ^{[1
]}

Garcia, R. ^{[2
]}

机构：

[1] Univ Autonoma Madrid, Dept Fis Mat Condensada, E-28049 Madrid, Spain

[2] IMM CNM CSIC, Inst Microelect Madrid, Madrid 28760, Spain

来源：

PHYSICAL REVIEW LETTERS | 2011年 / 106卷 / 19期

关键词：

SPECTROSCOPY; RESOLUTION; SURFACES; MODE;

D O I：

10.1103/PhysRevLett.106.198101

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

Mapping of the protein structural flexibility with sub-2-nm spatial resolution in liquid is achieved by combining bimodal excitation and frequency modulation force microscopy. The excitation of two cantilever eigenmodes in dynamic force microscopy enables the separation between topography and flexibility mapping. We have measured variations of the elastic modulus in a single antibody pentamer from 8 to 18 MPa when the probe is moved from the end of the protein arm to the central protrusion. Bimodal dynamic force microscopy enables us to perform the measurements under very small repulsive loads (30-40 pN).

引用

页数：4

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