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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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Related Experiment Video

Updated: Apr 24, 2026

Visualization of Recombinant DNA and Protein Complexes Using Atomic Force Microscopy
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Visualization of Recombinant DNA and Protein Complexes Using Atomic Force Microscopy

Published on: July 18, 2011

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Factor Va alternative conformation reconstruction using atomic force microscopy.

R C Chaves, S Dahmane, M Odorico

  • 1Jean-Luc Pellequer, IBS, Univ. Grenoble Alpes/CNRS/CEA, 71 avenue des Martyrs CS 10090 F-38044 Grenoble, Cedex 9, France,

Thrombosis and Haemostasis
|September 5, 2014
PubMed
Summary
This summary is machine-generated.

Protein conformational dynamics are crucial for biological function. This study reveals significant angle variations between human coagulation factor Va

Keywords:
Coagulation factorsatomic force microscopyimagingphospholipidsprotein structure / folding

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Structural Biology

Background:

  • Protein conformational variability influences biological function.
  • Collective domain motions enhance protein-partner binding.
  • Atomic Force Microscopy (AFM) enables single-molecule imaging of macromolecules.

Purpose of the Study:

  • To characterize the conformational variability of human coagulation factor Va (FVa) C domains.
  • To apply the AFM-assembly reconstruction protocol for detailed molecular analysis.

Main Methods:

  • Utilized Atomic Force Microscopy (AFM) to obtain topographic images of FVa in a liquid environment.
  • Applied the AFM-assembly protocol to reconstruct complete molecular conformations from AFM data.

Main Results:

  • Demonstrated significant conformational variability in FVa.
  • Quantified the angle between the C1 and C2 domains of FVa, ranging from 40° to 166°.

Conclusions:

  • The dynamic arrangement of FVa's C1 and C2 domains may impact its binding to phospholipid membranes.
  • Understanding protein dynamics is key to elucidating molecular mechanisms.