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Viscoelasticity of single folded proteins using dynamic atomic force microscopy.

Surya Pratap S Deopa1, Shivprasad Patil1

  • 1Department of Physics, Indian Institute of Science Education and Research, Pune, India. s.patil@iiserpune.ac.in.

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Single molecule force spectroscopy uses atomic force microscopy to measure protein viscoelasticity. New methods offer promising insights into protein dynamics and structural flexibility, overcoming previous measurement challenges.

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Area of Science:

  • Biophysics
  • Materials Science
  • Biochemistry

Background:

  • Single molecule force spectroscopy enables measurement of protein responses to mechanical forces.
  • Techniques like atomic force microscopy (AFM) and optical tweezers are pivotal in this field.
  • Quantifying protein viscoelasticity is crucial for understanding protein dynamics.

Purpose of the Study:

  • To review efforts in measuring protein viscoelasticity using dynamic AFM.
  • To identify challenges and pitfalls in artifact-free viscoelasticity measurements.
  • To discuss novel methods for assessing protein viscoelasticity and their implications.

Main Methods:

  • Application of controlled forces (pN to nN) to single protein domains.
  • Clamp-type experiments measuring unfolding force and time distributions.
  • Sinusoidal force application to quantify elastic and viscous responses (viscoelasticity).

Main Results:

  • AFM has advanced the study of single protein mechanical responses.
  • Measuring protein viscoelasticity using dynamic AFM presents significant challenges.
  • A new promising method has been reported for measuring folded protein viscoelasticity.

Conclusions:

  • Despite technical advances, artifact-free measurement of protein viscoelasticity remains difficult.
  • Understanding protein viscoelasticity is key to comprehending protein dynamics and flexibility.
  • Emerging techniques promise more accurate assessments of protein mechanical properties.