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

Proteins in a shear flow.

P Szymczak1, Marek Cieplak

  • 1Institute of Theoretical Physics, Warsaw University, ul. Hoza 69, 00-681 Warsaw, Poland. piotrek@fuw.edu.pl

The Journal of Chemical Physics
|October 24, 2007
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

Stress resilience is an active and multifactorial process manifested by structural, functional, and molecular changes in synapses.

Neurobiology of stress·2024
Same author

Dislike of general opinion makes for tight elections.

Physical review. E·2024
Same author

The coexistence region in the Van der Waals fluid and the liquid-liquid phase transitions.

Frontiers in chemistry·2023
Same author

Contact-Based Analysis of Aggregation of Intrinsically Disordered Proteins.

Methods in molecular biology (Clifton, N.J.)·2022
Same author

Final Remarks.

Methods in molecular biology (Clifton, N.J.)·2022
Same author

Preface to the JPCM special issue on droplets and vesicles.

Journal of physics. Condensed matter : an Institute of Physics journal·2021
Same journal

Anharmonic phonons via quantum thermal bath simulations.

The Journal of chemical physics·2026
Same journal

Quantum simulation of alignment dependent differential cross sections in co-propagating molecular beams at cold collision energies.

The Journal of chemical physics·2026
Same journal

Non-additive ion effects on the coil-globule equilibrium of a generic polymer in aqueous salt solutions.

The Journal of chemical physics·2026
Same journal

Insights into the unexpected small reduction of the temperature of maximum density of water by lithium chloride addition.

The Journal of chemical physics·2026
Same journal

Optical frequency comb double-resonance spectroscopy of the 9030-9175 cm-1 states of ethylene.

The Journal of chemical physics·2026
Same journal

Time reversal breaking of colloidal particles in cells.

The Journal of chemical physics·2026
See all related articles

Single protein unfolding in shear flow reveals distinct intermediate states, unlike smooth homopolymer unraveling. Hydrodynamic interactions and anchoring points significantly influence this complex process.

Area of Science:

  • Biophysics
  • Computational Biology
  • Protein Dynamics

Background:

  • Understanding protein conformational changes under external forces is crucial for molecular biology.
  • Shear flow is a relevant physical condition encountered in biological systems and industrial processes.
  • Previous studies on homopolymers showed smooth unraveling, but protein-specific behavior remained less understood.

Purpose of the Study:

  • To investigate the conformational dynamics and unfolding mechanisms of single protein molecules subjected to shear flow.
  • To elucidate the role of protein structure, hydrodynamic interactions, and anchoring in shear-induced unfolding.
  • To compare the unfolding patterns of globular proteins with those of homopolymers.

Main Methods:

  • Brownian dynamics simulations were employed to model protein behavior.

Related Experiment Videos

  • A structure-based coarse-grained model was utilized for representing protein molecules.
  • Simulations were performed on two specific proteins: ubiquitin and integrin.
  • Main Results:

    • Proteins like ubiquitin and integrin exhibit unfolding through a series of metastable states at moderate shear rates, differing from homopolymer behavior.
    • Complete unfolding requires very high shear rates.
    • Hydrodynamic interactions between amino acids were found to impede the unfolding process.
    • The unfolding pathway is sensitive to whether the protein is anchored and the specific anchoring site.

    Conclusions:

    • Single protein unfolding in shear flow is a complex, multi-state process distinct from simple polymer unraveling.
    • Protein structure and interactions play a critical role in determining the response to shear forces.
    • Anchoring conditions significantly modulate protein conformational dynamics under flow, offering insights into protein stability and function in dynamic environments.