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

Atomic force microscopy captures length phenotypes in single proteins.

M Carrion-Vazquez1, P E Marszalek, A F Oberhauser

  • 1Department of Physiology, Mayo Foundation, Rochester, MN 55905, USA.

Proceedings of the National Academy of Sciences of the United States of America
|September 29, 1999
PubMed
Summary
This summary is machine-generated.

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

Activation of AGEs-RAGE axis impairs bone repair in a metabolic syndrome model.

Molecular and cellular endocrinology·2026
Same author

X-chromosomal STRs: Metapopulations and mutation rates.

Forensic science international. Genetics·2025
Same author

Alginate-HEMA Hydrogels as Promising Biomaterials for Bone Regeneration: In Vitro and In Vivo Studies.

Journal of biomedical materials research. Part B, Applied biomaterials·2024
Same author

Laboratory study of rotationally inelastic collisions of CO2 at low temperatures.

The Journal of chemical physics·2024
Same author

Embryonic cerebrospinal fluid influence in the subependymal neurogenic niche in adult mouse hippocampus.

Tissue & cell·2023
Same author

Urinary pH and antibiotics, choose carefully. A systematic review.

Actas urologicas espanolas·2023

Single-protein atomic force microscopy precisely measures protein length changes. Specific glycine insertions in the Ig module core extend its length by 20 Å, demonstrating high-resolution structural analysis.

Area of Science:

  • Biophysics
  • Structural Biology
  • Protein Engineering

Background:

  • Understanding protein structure-function relationships is crucial.
  • Atomic force microscopy (AFM) offers a powerful tool for single-molecule analysis.
  • Ig modules are common protein structural units with diverse functions.

Purpose of the Study:

  • To develop and apply single-protein AFM techniques for precise length measurements of Ig modules.
  • To investigate the impact of specific amino acid insertions on protein extension.
  • To demonstrate the capability of AFM for high-resolution structural characterization.

Main Methods:

  • Utilizing single-protein atomic force microscopy (AFM) to probe mechanical unfolding.
  • Engineering polyproteins comprising up to 12 tandem Ig module repeats.

Related Experiment Videos

  • Analyzing extension differences between wild-type and mutant polyproteins upon mechanical unfolding.

    • Main Results:

    • AFM successfully detected length variations in single Ig modules.
    • Polyproteins with five glycine residues inserted into the Ig module core extended 20 Å further per module compared to wild-type.
    • Insertions near the N or C termini did not significantly alter polyprotein extension.

    Conclusions:

    • Single-protein AFM can accurately detect and quantify length changes in proteins at the amino acid level.
    • The location of amino acid insertions critically influences their effect on protein extension.
    • AFM provides a complementary high-resolution structural analysis method comparable to NMR and X-ray crystallography.