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Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope
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Directly measuring single-molecule heterogeneity using force spectroscopy.

Michael Hinczewski1, Changbong Hyeon2, D Thirumalai3

  • 1Department of Physics, Case Western Reserve University, Cleveland, OH 44106; mxh605@case.edu.

Proceedings of the National Academy of Sciences of the United States of America
|June 19, 2016
PubMed
Summary
This summary is machine-generated.

Functional heterogeneity, where cellular machines adopt multiple conformations, is widespread. New analysis of single-molecule experiments reveals this phenomenon and its slow conformational switching times.

Keywords:
atomic force microscopebiomolecule heterogeneitydynamic disorderoptical tweezersrupture force distribution

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Area of Science:

  • Biophysics
  • Single-molecule biophysics
  • Structural biology

Background:

  • Single-molecule experiments reveal functional heterogeneity in cellular machines.
  • This heterogeneity involves multiple, long-lived conformations with slow interconversions.
  • Identifying and measuring this phenomenon remains challenging.

Purpose of the Study:

  • To demonstrate the widespread nature of functional heterogeneity.
  • To develop a theoretical procedure for analyzing single-molecule pulling experiment data.
  • To quantify heterogeneity and estimate conformational interconversion timescales.

Main Methods:

  • Analysis of rupture/unfolding force distributions from atomic force microscopy and optical tweezer pulling experiments.
  • Development of a theoretical procedure to analyze data at different pulling speeds.
  • Application of the procedure to 10 published datasets.

Main Results:

  • Evidence of functional heterogeneity found in 5 out of 10 analyzed datasets.
  • Identified heterogeneity is associated with interconversion rates slower than 10 s⁻¹.
  • Two systems identified where a crossover regime between heterogeneous and non-heterogeneous behavior may be observed.

Conclusions:

  • Functional heterogeneity is more prevalent than previously thought.
  • The developed method quantifies heterogeneity and provides bounds on timescales.
  • Further experiments in specific systems could yield precise estimates of slow conformational switching times.