Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Mapping flexible protein domains at subnanometer resolution with the atomic force microscope

D J Müller1, D Fotiadis, A Engel

  • 1M.E. Müller-Institute for Microscopy, Biozentrum, University of Basel, Switzerland.

FEBS Letters
|July 25, 1998
PubMed
Summary

Atomic force microscopy maps flexible protein domains, revealing reversible structural changes in key biomolecules. This technique correlates surface features with polypeptide loops, offering insights into protein dynamics.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Conditional progression-free survival in patients with metastatic hormone receptor-positive, human epidermal growth factor receptor 2-negative breast cancer treated with first-line ribociclib and endocrine therapy: real-world data from the RIBANNA study.

ESMO open·2025
Same author

Coupled FEA Model with Continuum Damage Mechanics for the Degradation of Polymer-based coatings on Drug-Eluting Stents.

Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Annual International Conference·2021
Same author

FEA of Drug-Eluting Stents and Sensitivity Analysis of a Continuum Damage Model for the Degradation of PLGA Coating.

Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Annual International Conference·2021
Same author

A region within the third extracellular loop of rat Aquaporin 6 precludes trafficking to plasma membrane in a heterologous cell line.

Scientific reports·2021
Same author

MTT Heterogeneity in Perfusion CT Imaging as a Predictor of Outcome after Aneurysmal SAH.

AJNR. American journal of neuroradiology·2021
Same author

Designing a mHealth clinical decision support system for Parkinson's disease: a theoretically grounded user needs approach.

BMC medical informatics and decision making·2020

Area of Science:

  • Biophysics
  • Structural Biology
  • Microscopy

Background:

  • Flexible protein domains play crucial roles in biological functions.
  • Understanding protein dynamics requires high-resolution imaging techniques.
  • Atomic Force Microscopy (AFM) offers potential for studying protein structures in near-native conditions.

Purpose of the Study:

  • To review the application of AFM for mapping flexible protein domains.
  • To demonstrate the capability of AFM in visualizing dynamic structural changes in proteins.
  • To correlate observed surface features with specific molecular structures like polypeptide loops.

Main Methods:

  • Atomic Force Microscopy (AFM) was employed to image protein complexes.
  • Proteins were imaged in physiological buffer solutions to mimic native environments.

Related Experiment Videos

  • Standard deviation maps were calculated from aligned topographs to highlight flexibility.
  • Multivariate statistical classification was used to analyze major protein conformations.

    • Main Results:

    • AFM successfully mapped flexible protein domains of bacteriorhodopsin, phage phi29 head-tail-connector, and Deinococcus radiodurans intermediate layer.
    • Reversible structural changes were observed and quantified in these proteins.
    • High lateral resolution (up to 0.8 nm) allowed correlation of surface regions with individual polypeptide loops.
    • Multivariate statistical analysis identified distinct protein conformations.

    Conclusions:

    • AFM is a powerful tool for characterizing the dynamics and structural flexibility of proteins.
    • The study provides atomic-level insights into the conformational states of complex biomolecules.
    • Visualizing protein flexibility in physiological conditions advances our understanding of molecular mechanisms.