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

Random sequences with power-law correlations exhibit proteinlike behavior.

Yevgeni Sh Mamasakhlisov1, Shura Hayryan, Chin-Kun Hu

  • 1Institute of Physics, Academia Sinica, Nankang, Taipei 11529, Taiwan.

The Journal of Chemical Physics
|April 21, 2007
PubMed
Summary

Random heteropolymers with persistent power-law correlations exhibit protein-like folding properties. They fold into unique structures via fast or slow pathways, with the latter involving microphase separated (MPS) states.

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

Universality and scaling in complex networks from periods of Chinese history.

Chaos (Woodbury, N.Y.)·2023
Same author

Computational Design of Gas Sensors Based on V<sub>3</sub>S<sub>4</sub> Monolayer.

Nanomaterials (Basel, Switzerland)·2022
Same author

Polymorphism in rapidly changing cyclic environment.

Physical review. E·2019
Same author

Specific heat and partition function zeros for the dimer model on the checkerboard B lattice: Finite-size effects.

Physical review. E·2019
Same author

Dependence of extreme events on spatial location.

Physical review. E·2018
Same author

Circuit variability interacts with excitatory-inhibitory diversity of interneurons to regulate network encoding capacity.

Scientific reports·2018

Area of Science:

  • Statistical mechanics
  • Polymer physics
  • Biophysics

Background:

  • Random heteropolymers are models for complex polymers.
  • Understanding protein folding pathways is crucial in biophysics.

Purpose of the Study:

  • Investigate thermodynamic properties of random heteropolymers with power-law correlations.
  • Determine if these sequences exhibit protein-like folding behaviors.

Main Methods:

  • Utilized a replica approach to analyze polymer thermodynamics.
  • Calculated the scale and magnitude of microphase separated (MPS) states.

Main Results:

  • Demonstrated that these heteropolymers possess protein-like properties.
  • Identified two distinct folding pathways: direct to native state and via intermediate glassy/MPS states.

Related Experiment Videos

  • Determined conditions for reaching a frozen state based on correlation strength.

    • Conclusions:

    • Heteropolymers with persistent power-law correlations can fold into stable native structures.
    • Folding pathways are dependent on the strength of long-range correlations in the monomer sequence.