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Related Concept Videos

Atomic Force Microscopy01:08

Atomic Force Microscopy

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Atomic force microscopy (AFM) is a type of scanning probe microscopy that can analyze topographic details of various specimens like ceramics, glass, polymers, and biological samples. AFM offers over 1000 times more resolution than the optical imaging system. Images generated from AFM are three-dimensional surface profiles, offering an advantage over the flat, two-dimensional images from other imaging techniques.
The AFM Probe
The probe is regarded as the heart of any AFM setup and comprises the...
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Sub-nanometer Resolution Imaging with Amplitude-modulation Atomic Force Microscopy in Liquid
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The nano-scale viscoelasticity using atomic force microscopy in liquid environment.

Shatruhan Singh Rajput1, Surya Pratap S Deopa1, Jyoti Yadav2

  • 1Department of Physics, Indian Institute of Science Education and Research Pune, Dr. Homi Bhabha Road, Pashan, Pune 411008, India.

Nanotechnology
|October 29, 2020
PubMed
Summary
This summary is machine-generated.

This study reveals that single protein molecules exhibit immeasurably low dissipation, challenging previous findings. Atomic force microscopy measurements highlight potential artifacts in conventional methods for quantifying nanoscale viscoelasticity.

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Area of Science:

  • Nanoscale science
  • Biophysics
  • Physical chemistry

Background:

  • Quantifying viscoelasticity in nanoscale systems is crucial for understanding molecular behavior.
  • Previous studies reported significant dissipation in single protein molecules, but experimental limitations may have contributed to these findings.
  • Atomic force microscopy (AFM) is a key technique for probing mechanical properties at the nanoscale.

Purpose of the Study:

  • To accurately measure the viscoelasticity of single protein molecules and confined water layers.
  • To investigate and identify sources of artifacts in AFM-based dissipation measurements.
  • To compare the performance of different AFM detection schemes for viscoelasticity measurements.

Main Methods:

  • Utilized two AFM detection schemes: commercial deflection detection (cantilever bending) and fiber-interferometer based detection (cantilever displacement).
  • Modeled cantilever hydrodynamics using the Euler-Bernoulli equation to account for different detection methods.
  • Performed measurements on single octomers of titin (I27 b8) and molecular layers of water confined between solid surfaces.

Main Results:

  • The dissipation coefficient of single titin I27 b8 was found to be immeasurably low (upper bound 5 × 10 b-7 kg s b-1), contradicting literature values.
  • Entropic stiffness of single unfolded protein domains was measured at approximately 10 mN m b-1 using both methods.
  • Identified phase artifacts in conventional deflection detection as a major source of error in dissipation estimates.

Conclusions:

  • Cantilever displacement measurement offers superior accuracy for artifact-free viscoelasticity measurements compared to bending detection, especially at low frequencies.
  • The low dissipation observed in single protein molecules suggests a need to re-evaluate their role in energy dissipation mechanisms.
  • Findings provide insights into discrepancies in protein collapse dynamics observed between force spectroscopy and optical techniques.