Measuring AFM cantilever stiffness from a thermal noise spectrum

Malovichko, Ivan

doi:10.3103/s1062873813080248

Cited by 4 publications

(2 citation statements)

References 7 publications

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“…Since high-precision sensors typically operate on or near resonance for increased gain, thermal noise limits their sensitivities. Because of its ubiquity, thermal noise is widely used for calibration (12)(13)(14) and measurement (15)(16)(17) of nanomechanical sensors. For example, in conventional AFM setups, thermal noise is typically well above detection noise at frequencies near the AFM cantilever resonances and it is used to obtain the probe's mechanical properties.…”

Section: Introductionmentioning

confidence: 99%

Beating thermal noise in a dynamic signal measurement by a nanofabricated cavity optomechanical sensor

et al. 2023

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Thermal fluctuations often impose both fundamental and practical measurement limits on high-performance sensors, motivating the development of techniques that bypass the limitations imposed by thermal noise outside cryogenic environments. Here, we theoretically propose and experimentally demonstrate a measurement method that reduces the effective transducer temperature and improves the measurement precision of a dynamic impulse response signal. Thermal noise–limited, integrated cavity optomechanical atomic force microscopy probes are used in a photothermal-induced resonance measurement to demonstrate an effective temperature reduction by a factor of ≈25, i.e., from room temperature down as low as ≈12 K, without cryogens. The method improves the experimental measurement precision and throughput by >2×, approaching the theoretical limit of ≈3.5× improvement for our experimental conditions. The general applicability of this method to dynamic measurements leveraging thermal noise–limited harmonic transducers will have a broad impact across a variety of measurement platforms and scientific fields.

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Section: Introductionmentioning

confidence: 99%

Beating thermal noise in a dynamic signal measurement by a nanofabricated cavity optomechanical sensor

et al. 2023

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“…The determination of probe spring constants dates back to the 1990s [9][10][11][12][13]. Common methods for the determination of cantilever probe spring constant are based on calculation from dimension and material properties [14], the use of a reference cantilever [15,16], added mass [9,17], and thermal noise analysis [18,19].…”

Section: Introductionmentioning

confidence: 99%

Mechanical Characterization of Torsional Micropaddles Using Atomic Force Microscopy

et al. 2018

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The reference cantilever method is shown to act as a direct and simple method for determination of torsional spring constant. It has been applied to the characterization of micropaddle structures similar to those proposed for resonant functionalized chemical sensors and resonant thermal detectors. It is shown that this method can be used as an effective procedure to characterize a key parameter of these devices and would be applicable to characterization of other similar MEMS/NEMS devices such as micromirrors. In this study, two sets of micropaddles are manufactured (beams at centre and offset by 2.5 μm) by using LPCVD silicon nitride as a substrate. The patterning is made by direct milling using focused ion beam. The torsional spring constant is achieved through micromechanical analysis via atomic force microscopy. To obtain the gradient of force curve, the area of the micropaddle is scanned and the behaviour of each pixel is investigated through an automated developed code. The experimental results are in a good agreement with theoretical results.

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The physics of pulling polyproteins: a review of single molecule force spectroscopy using the AFM to study protein unfolding

2016

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One of the most exciting developments in the field of biological physics in recent years is the ability to manipulate single molecules and probe their properties and function. Since its emergence over two decades ago, single molecule force spectroscopy has become a powerful tool to explore the response of biological molecules, including proteins, DNA, RNA and their complexes, to the application of an applied force. The force versus extension response of molecules can provide valuable insight into its mechanical stability, as well as details of the underlying energy landscape. In this review we will introduce the technique of single molecule force spectroscopy using the atomic force microscope (AFM), with particular focus on its application to study proteins. We will review the models which have been developed and employed to extract information from single molecule force spectroscopy experiments. Finally, we will end with a discussion of future directions in this field.

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Measuring AFM cantilever stiffness from a thermal noise spectrum

Cited by 4 publications

References 7 publications

Beating thermal noise in a dynamic signal measurement by a nanofabricated cavity optomechanical sensor

Beating thermal noise in a dynamic signal measurement by a nanofabricated cavity optomechanical sensor

Mechanical Characterization of Torsional Micropaddles Using Atomic Force Microscopy

The physics of pulling polyproteins: a review of single molecule force spectroscopy using the AFM to study protein unfolding

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