The noise of coated cantilevers

Labuda, Aleksander; Bates, Jeffrey R.; Grütter, Peter

doi:10.1088/0957-4484/23/2/025503

Cited by 30 publications

(33 citation statements)

References 92 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This result is consistent with prior work using a variety of cantilevers and conditions ( e.g. , cantilevers coated on one side in liquid, 14,15,18 and partially 19 or fully 16 coated on one side in air).…”

supporting

confidence: 91%

Routine and Timely Sub-picoNewton Force Stability and Precision for Biological Applications of Atomic Force Microscopy

et al. 2012

View full text Add to dashboard Cite

Force drift is a significant, yet unresolved, problem in atomic force microscopy (AFM). We show that the primary source of force drift for a popular class of cantilevers is their gold coating, even though they are coated on both sides to minimize drift. Drift of the zero-force position of the cantilever was reduced from 900 nm for gold-coated cantilevers to 70 nm (N =10; rms) for uncoated cantilevers over the first 2 hours after wetting the tip; a majority of these uncoated cantilevers (60%) showed significantly less drift (12 nm, rms). Removing the gold also led to ~10-fold reduction in reflected light, yet short-term (0.1–10 s) force precision improved. Moreover, improved force precision did not require extended settling; most of the cantilevers tested (9 out of 15) achieved sub-pN force precision (0.54 ± 0.02 pN) over a broad bandwidth (0.01–10 Hz) just 30 min after loading. Finally, this precision was maintained while stretching DNA. Hence, removing gold enables both routine and timely access to sub-pN force precision in liquid over extended periods (100 s). We expect that many current and future applications of AFM can immediately benefit from these improvements in force stability and precision.

show abstract

supporting

confidence: 91%

Routine and Timely Sub-picoNewton Force Stability and Precision for Biological Applications of Atomic Force Microscopy

et al. 2012

View full text Add to dashboard Cite

show abstract

“…For SMFS experiments the cantilever spring constant must be soft enough to respond to the piconewtons forces observed for protein unfolding events, typically between 6 -100 pNnm -1 The force sensitivity of a cantilever is limited by its thermal noise [72] therefore cantilevers with low spring constants (softer) are more susceptible to noise [73]. Measurements using the AFM are limited by instrument stability and force sensitivity making the measurement of small forces over long periods of time challenging.…”

Section: Calibration Of the Cantilevermentioning

confidence: 99%

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

2016

View full text Add to dashboard Cite

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.

show abstract

“…In this paper, we focus on one design parameter, namely, the level of damping in miniaturized mechanical resonators. Controlling damping is a ubiquitous and vital requirement because miniaturized resonators require high quality factors (Q > 10 4 ) or ultrahigh quality factors (Q > 10 6 ) for optimal performance [16][17][18][19]. The former is typical of MEMS used for signal processing and inertial sensing [16], and the latter of miniaturized resonators used for precision measurements [6].…”

Section: Devices Applications and Design Parametersmentioning

confidence: 99%

Design strategies for controlling damping in micromechanical and nanomechanical resonators

2014

View full text Add to dashboard Cite

Damping is a critical design parameter for miniaturized mechanical resonators usedin microelectromechanical systems (MEMS), nanoelectromechanical systems (NEMS),optomechanical systems, and atomic force microscopy for a large and diverse set ofapplications ranging from sensing, timing, and signal processing to precisionmeasurements for fundamental studies of materials science and quantum mechanics.This paper presents an overview of recent advances in damping from the viewpointof device design. The primary goal is to collect and organize methods, tools, andtechniques for the rational and effective control of linear damping in miniaturizedmechanical resonators. After reviewing some fundamental links between dynamicsand dissipation for systems with small linear damping, we explore the space ofdesign and operating parameters for micromechanical and nanomechanicalresonators; classify the mechanisms of dissipation into fluid–structure interactions(viscous damping, squeezed-film damping, and acoustic radiation), boundarydamping (stress-wave radiation, microsliding, and viscoelasticity), and materialdamping (thermoelastic damping, dissipation mediated by phonons and electrons,and internal friction due to crystallographic defects); discuss strategies for minimizingeach source using a combination of models for dissipation and measurements of material properties; and formulate design principles for low-loss micromechanical and nanomechanical resonators

show abstract

The noise of coated cantilevers

Cited by 30 publications

References 92 publications

Routine and Timely Sub-picoNewton Force Stability and Precision for Biological Applications of Atomic Force Microscopy

Routine and Timely Sub-picoNewton Force Stability and Precision for Biological Applications of Atomic Force Microscopy

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

Design strategies for controlling damping in micromechanical and nanomechanical resonators

Contact Info

Product

Resources

About