BioAFMviewer: An interactive interface for simulated AFM scanning of biomolecular structures and dynamics

PLoS Comput Biol. 2020 Nov 18;16(11):e1008444. doi: 10.1371/journal.pcbi.1008444. eCollection 2020 Nov.

Abstract

We provide a stand-alone software, the BioAFMviewer, which transforms biomolecular structures into the graphical representation corresponding to the outcome of atomic force microscopy (AFM) experiments. The AFM graphics is obtained by performing simulated scanning over the molecular structure encoded in the corresponding PDB file. A versatile molecular viewer integrates the visualization of PDB structures and control over their orientation, while synchronized simulated scanning with variable spatial resolution and tip-shape geometry produces the corresponding AFM graphics. We demonstrate the applicability of the BioAFMviewer by comparing simulated AFM graphics to high-speed AFM observations of proteins. The software can furthermore process molecular movies of conformational motions, e.g. those obtained from servers which model functional transitions within a protein, and produce the corresponding simulated AFM movie. The BioAFMviewer software provides the platform to employ the plethora of structural and dynamical data of proteins in order to help in the interpretation of biomolecular AFM experiments.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Computational Biology
  • Computer Graphics
  • Computer Simulation
  • Microscopy, Atomic Force / statistics & numerical data*
  • Microscopy, Video / statistics & numerical data
  • Molecular Dynamics Simulation / statistics & numerical data
  • Molecular Structure
  • Motion Pictures
  • Nanotechnology
  • Protein Conformation
  • Proteins / chemistry
  • Proteins / ultrastructure
  • Software*
  • User-Computer Interface

Substances

  • Proteins

Grants and funding

H.F. acknowledges support by the Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan (https://www.mext.go.jp), through the World Premier International Research Center (WPI) Initiative. This work was supported by WPI-NanoLSI Transdisciplinary Research Promotion Grants, Kanazawa University. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.